Teru Ogura

Summary

Affiliation: Kumamoto University
Country: Japan

Publications

  1. ncbi request reprint Caenorhabditis elegans p97 controls germline-specific sex determination by controlling the TRA-1 level in a CUL-2-dependent manner
    Yohei Sasagawa
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    J Cell Sci 122:3663-72. 2009
  2. ncbi request reprint [Protein recycling systems in prokaryotic cells]
    Teru Ogura
    Tanpakushitsu Kakusan Koso 49:1047-53. 2004
  3. ncbi request reprint [AAA proteins as unfoldases]
    Teru Ogura
    Tanpakushitsu Kakusan Koso 49:1044-6. 2004
  4. ncbi request reprint Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases
    Teru Ogura
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
    J Struct Biol 146:106-12. 2004
  5. ncbi request reprint [AAA family ATPases: ring-shaped chaperones which catalyze energy-dependent conformational changes of proteins]
    Teru Ogura
    Tanpakushitsu Kakusan Koso 47:1182-8. 2002
  6. ncbi request reprint AAA+ superfamily ATPases: common structure--diverse function
    T Ogura
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
    Genes Cells 6:575-97. 2001
  7. ncbi request reprint Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli
    T Ogura
    Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
    Mol Microbiol 31:833-44. 1999
  8. ncbi request reprint From the common molecular basis of the AAA protein to various energy-dependent and -independent activities of AAA proteins
    Teru Ogura
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860 0811, Japan
    Biochem Soc Trans 36:68-71. 2008
  9. ncbi request reprint Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysis
    Tomoko Yamada-Inagawa
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
    J Biol Chem 278:50182-7. 2003
  10. ncbi request reprint Flavodoxin, a new fluorescent substrate for monitoring proteolytic activity of FtsH lacking a robust unfolding activity
    Takashi Okuno
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860 0811, Japan
    J Struct Biol 156:115-9. 2006

Collaborators

Detail Information

Publications60

  1. ncbi request reprint Caenorhabditis elegans p97 controls germline-specific sex determination by controlling the TRA-1 level in a CUL-2-dependent manner
    Yohei Sasagawa
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    J Cell Sci 122:3663-72. 2009
    ..Our results demonstrate that the C. elegans p97/CDC-48-UFD-1-NPL-4 complex controls the sperm-oocyte switch by regulating CUL-2-mediated TRA-1A proteasome degradation...
  2. ncbi request reprint [Protein recycling systems in prokaryotic cells]
    Teru Ogura
    Tanpakushitsu Kakusan Koso 49:1047-53. 2004
  3. ncbi request reprint [AAA proteins as unfoldases]
    Teru Ogura
    Tanpakushitsu Kakusan Koso 49:1044-6. 2004
  4. ncbi request reprint Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases
    Teru Ogura
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
    J Struct Biol 146:106-12. 2004
    ..In this review, we will discuss what is known about these critical arginines and what can be concluded about their role in the function of AAA and AAA+ proteins...
  5. ncbi request reprint [AAA family ATPases: ring-shaped chaperones which catalyze energy-dependent conformational changes of proteins]
    Teru Ogura
    Tanpakushitsu Kakusan Koso 47:1182-8. 2002
  6. ncbi request reprint AAA+ superfamily ATPases: common structure--diverse function
    T Ogura
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
    Genes Cells 6:575-97. 2001
    ..Comparative analyses have also revealed significant similarities and differences in structure and molecular mechanism between AAA+ ATPases and other ring-shaped ATPases...
  7. ncbi request reprint Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli
    T Ogura
    Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
    Mol Microbiol 31:833-44. 1999
    ..The biosynthesis of phospholipids and the lipid A moiety of lipopolysaccharide, both of which derive their fatty acyl chains from the same R-3-hydroxyacyl-ACP pool, is regulated by FtsH...
  8. ncbi request reprint From the common molecular basis of the AAA protein to various energy-dependent and -independent activities of AAA proteins
    Teru Ogura
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860 0811, Japan
    Biochem Soc Trans 36:68-71. 2008
    ..We have also investigated the roles of C. elegans p97 homologues in aggregation/disaggregation of polyglutamine repeats, and have found that p97 prevents filament formation of polyglutamine proteins in an ATP-independent fashion...
  9. ncbi request reprint Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysis
    Tomoko Yamada-Inagawa
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
    J Biol Chem 278:50182-7. 2003
    ..These results suggest that Phe228 and Gly230 in the predicted pore region of the FtsH hexamer have important roles in proteolysis and its coupling to ATP hydrolysis...
  10. ncbi request reprint Flavodoxin, a new fluorescent substrate for monitoring proteolytic activity of FtsH lacking a robust unfolding activity
    Takashi Okuno
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860 0811, Japan
    J Struct Biol 156:115-9. 2006
    ..This newly developed monitoring system will also be applicable for proteolysis by other ATP-dependent proteases...
  11. ncbi request reprint Spectrometric analysis of degradation of a physiological substrate sigma32 by Escherichia coli AAA protease FtsH
    Takashi Okuno
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
    J Struct Biol 146:148-54. 2004
    ..Although FtsH does not have a robust enough unfoldase activity to unfold a tightly folded proteins such as green fluorescent protein, it can unfold proteins with lower T(m)s such as glutathione S-transferase (T(m) = 52 degrees C)...
  12. ncbi request reprint ER E3 ubiquitin ligase HRD-1 and its specific partner chaperone BiP play important roles in ERAD and developmental growth in Caenorhabditis elegans
    Yohei Sasagawa
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    Genes Cells 12:1063-73. 2007
    ..We propose that E3 ubiquitin ligases function in concert with a specific partner chaperone...
  13. ncbi request reprint Mutational analysis of the functional motifs in the ATPase domain of Caenorhabditis elegans fidgetin homologue FIGL-1: firm evidence for an intersubunit catalysis mechanism of ATP hydrolysis by AAA ATPases
    Yasufumi Yakushiji
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    J Struct Biol 156:93-100. 2006
    ....
  14. ncbi request reprint An AAA protease FtsH can initiate proteolysis from internal sites of a model substrate, apo-flavodoxin
    Takashi Okuno
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860 0811, Japan
    Genes Cells 11:261-8. 2006
    ....
  15. doi request reprint Caenorhabditis elegans UBX cofactors for CDC-48/p97 control spermatogenesis
    Yohei Sasagawa
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    Genes Cells 15:1201-15. 2010
    ..Taken together, these results suggest that UBXN-1, UBXN-2 and UBXN-3 are redundant cofactors for CDC-48/p97 and control spermatogenesis via the degradation of TRA-1A...
  16. ncbi request reprint p97 Homologs from Caenorhabditis elegans, CDC-48.1 and CDC-48.2, suppress the aggregate formation of huntingtin exon1 containing expanded polyQ repeat
    Shingo Nishikori
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    Genes Cells 13:827-38. 2008
    ..1 and CDC-48.2. Taken together, these results suggest that p97 plays a protective role in neurodegenerative disorders by directly suppressing the protein aggregation as a molecular chaperone...
  17. pmc AAA+ chaperone ClpX regulates dynamics of prokaryotic cytoskeletal protein FtsZ
    Shinya Sugimoto
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    J Biol Chem 285:6648-57. 2010
    ..These data together suggest that ClpX modulates FtsZ polymer dynamics in an ATP-independent fashion, which is achieved by interaction between the N-terminal domain of ClpX and FtsZ monomers or oligomers...
  18. pmc Positive cooperativity of the p97 AAA ATPase is critical for essential functions
    Shingo Nishikori
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, Japan
    J Biol Chem 286:15815-20. 2011
    ..Interestingly, the growth speed of yeast cells strongly related to the positive cooperativity rather than the ATPase activity itself, suggesting that the positive cooperativity is critical for the essential functions of p97...
  19. doi request reprint A conserved α helix of Bcs1, a mitochondrial AAA chaperone, is required for the Respiratory Complex III maturation
    Rie Sawamura
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860 0811, Japan
    Biochem Biophys Res Commun 443:997-1002. 2014
    ..The evolutionarily-conserved short α helix of Bcs1 in the intermembrane space is an essential element for the chaperone function. ..
  20. ncbi request reprint High-speed atomic force microscopic observation of ATP-dependent rotation of the AAA+ chaperone p97
    Kentaro Noi
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860 0811, Japan The Global COE Cell Fate Regulation Research and Education Unit, Kumamoto University, Kumamoto 860 0811, Japan
    Structure 21:1992-2002. 2013
    ..In the presence of ATP, the N-D1 ring repeatedly rotates ~23 ± 8° clockwise and resets relative to the D2 ring. Mutational analysis reveals that this rotation is induced by ATP binding to the D2 domain...
  21. doi request reprint Caenorhabditis elegans fidgetin homolog FIGL-1, a nuclear-localized AAA ATPase, binds to SUMO
    Akinobu Onitake
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, Japan
    J Struct Biol 179:143-51. 2012
    ..elegans. Taken altogether, our results indicate that FIGL-1 is a nuclear protein and that in concert with SMO-1, FIGL-1 plays an important role in the regulation of C. elegans development...
  22. ncbi request reprint Characterization of mutants of the Escherichia coli AAA protease, FtsH, carrying a mutation in the central pore region
    Takashi Okuno
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860 0811, Japan
    J Struct Biol 156:109-14. 2006
    ..Proteolytic activities of most mutants are correlated with their ATPase activities. Evidence also indicated that Val229, the 2nd residue of the @XG motif, may have a substrate-specific role...
  23. ncbi request reprint Caenorhabditis elegans p97/CDC-48 is crucial for progression of meiosis I
    Yohei Sasagawa
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    Biochem Biophys Res Commun 358:920-4. 2007
    ..Furthermore, we found that chromosome condensation was significantly reduced in p97-depleted oocytes. Taken these results altogether, we propose that C. elegans p97 plays an important role in the progression of meiosis...
  24. doi request reprint The C-terminal α-helix of SPAS-1, a Caenorhabditis elegans spastin homologue, is crucial for microtubule severing
    Akinobu Onitake
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    J Struct Biol 179:138-42. 2012
    ....
  25. doi request reprint CDC-48/p97 is required for proper meiotic chromosome segregation via controlling AIR-2/Aurora B kinase localization in Caenorhabditis elegans
    Yohei Sasagawa
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    J Struct Biol 179:104-11. 2012
    ..However, the amount and localization of PP1 were not changed by the depletion of CDC-48s. These results suggest that CDC-48s control the restricted localization of AIR-2 to the cohesion sites of homologous chromatids in meiosis I...
  26. doi request reprint Conserved aromatic and basic amino acid residues in the pore region of Caenorhabditis elegans spastin play critical roles in microtubule severing
    Yuka Matsushita-Ishiodori
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    Genes Cells 14:925-40. 2009
    ..We also detected the direct interaction of the extremely acidic C-terminal polypeptide of tubulin with SPAS-1. Consequently, we propose that the central pore residues are important for the recognition of substrates...
  27. ncbi request reprint Involvement of HMG-12 and CAR-1 in the cdc-48.1 expression of Caenorhabditis elegans
    Seiji Yamauchi
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    Dev Biol 318:348-59. 2008
    ..Importantly, we found the decreased expression of p97 in embryos prepared from hmg-12(RNAi) or car-1(RNAi) worms. These results indicate that both HMG-12 and CAR-1 play important roles in embryonic expression of cdc-48.1...
  28. ncbi request reprint The C. elegans homologue of the spastic paraplegia protein, spastin, disassembles microtubules
    Yuka Matsushita-Ishiodori
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    Biochem Biophys Res Commun 359:157-62. 2007
    ..These results indicate that C. elegans SPAS-1 plays an important role in microtubule dynamics. We also found that two kinds of products were generated from spas-1 by alternative splicing in a developmental stage-dependent manner...
  29. ncbi request reprint Dissecting various ATP-dependent steps involved in proteasomal degradation
    Teru Ogura
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860 0976, Japan
    Mol Cell 11:3-5. 2003
    ..ATP hydrolysis, activated by binding of substrates to PAN, is utilized for substrate unfolding, gate opening of 20S proteasomes, and substrate translocation...
  30. ncbi request reprint Differential expression pattern of UBX family genes in Caenorhabditis elegans
    Seiji Yamauchi
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto, Japan
    Biochem Biophys Res Commun 358:545-52. 2007
    ..These results altogether demonstrate that the expression of all six ubxn genes of C. elegans is differently regulated...
  31. pmc The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression
    T Tomoyasu
    Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
    J Bacteriol 175:1344-51. 1993
    ..g., Sec18p, Pas1p, CDC48p, and TBP-1, which function in protein transport pathways, peroxisome assembly, cell division cycle, and gene expression, respectively. Possible implications of these observations are discussed...
  32. ncbi request reprint Heat shock regulation in the ftsH null mutant of Escherichia coli: dissection of stability and activity control mechanisms of sigma32 in vivo
    T Tatsuta
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kumamoto 862 0976, Japan
    Mol Microbiol 30:583-93. 1998
    ..In addition, CbpA, an analogue of DnaJ, was demonstrated to have overlapping functions with DnaJ in both the activity and the stability control of sigma32...
  33. ncbi request reprint Defective plasmid partition in ftsH mutants of Escherichia coli
    T Inagawa
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Japan
    Mol Genet Genomics 265:755-62. 2001
    ..It is likely that altered membrane structure affects the localization or activity of a putative plasmid partitioning apparatus located at positions equivalent to 1/4 and 3/4 of the cell length...
  34. ncbi request reprint Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH
    K Karata
    Department of Molecular Cell Biology, Institute of Molecular Embryology, Kumamoto University School of Medicine, Kumamoto 862 0976, Japan
    J Biol Chem 274:26225-32. 1999
    ....
  35. pmc Topology and subcellular localization of FtsH protein in Escherichia coli
    T Tomoyasu
    Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
    J Bacteriol 175:1352-7. 1993
    ..The average number of FtsH molecules per cell was estimated to be approximately 400...
  36. ncbi request reprint Analysis of the two p97/VCP/Cdc48p proteins of Caenorhabditis elegans and their suppression of polyglutamine-induced protein aggregation
    Kunitoshi Yamanaka
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
    J Struct Biol 146:242-50. 2004
    ..The formation of aggregates was partially suppressed by co-expression of either C41C4.8 or C06A1.1. These results suggest that these p97/VCP/Cdc48p homologues, AAA chaperones, may play a protective role in polyQ aggregation...
  37. ncbi request reprint Comparative analysis of expression of two p97 homologues in Caenorhabditis elegans
    Seiji Yamauchi
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    Biochem Biophys Res Commun 345:746-53. 2006
    ..2::GFP was expressed mainly in embryos. These results suggest that the expression of two p97 homologues of C. elegans is differently regulated and independent of each other...
  38. ncbi request reprint Probing the mechanism of ATP hydrolysis and substrate translocation in the AAA protease FtsH by modelling and mutagenesis
    K Karata
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
    Mol Microbiol 39:890-903. 2001
    ..Furthermore, comparative structural analysis of FtsH and a related ATPase, HslU, reveals interesting similarities and differences in mechanism...
  39. ncbi request reprint Identification of two new genes, mukE and mukF, involved in chromosome partitioning in Escherichia coli
    K Yamanaka
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Japan
    Mol Gen Genet 250:241-51. 1996
    ..These results indicate that the MukF, MukE, and MukB proteins are involved in the chromosome partitioning steps, but are not required for mini-F plasmid partitioning...
  40. doi request reprint Cdc48p/p97-mediated regulation of mitochondrial morphology is Vms1p-independent
    Masatoshi Esaki
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Honjo 2 2 1, Kumamoto 860 0811, Japan
    J Struct Biol 179:112-20. 2012
    ..These results suggest that Cdc48p controls mitochondrial morphology by regulating turnover of proteins involved in mitochondrial morphology in a Vms1p-independent manner...
  41. pmc Phosphorylation of Kif26b promotes its polyubiquitination and subsequent proteasomal degradation during kidney development
    Takeshi Terabayashi
    Department of Kidney Development, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto, Japan
    PLoS ONE 7:e39714. 2012
    ..These results suggest that the function of Kif26b is microtubule-based and that Kif26b degradation in the metanephric mesenchyme via the ubiquitin-proteasome pathway may be important for proper kidney development...
  42. doi request reprint Recent advances in p97/VCP/Cdc48 cellular functions
    Kunitoshi Yamanaka
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    Biochim Biophys Acta 1823:130-7. 2012
    ..In this review, we will summarize and discuss recent progress and topics in p97 functions and the relationship to its associated diseases...
  43. doi request reprint ATP-bound form of the D1 AAA domain inhibits an essential function of Cdc48p/p97
    Masatoshi Esaki
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, 2 2 1 Honjo, Kumamoto 860 0811, Japan
    Biochem Cell Biol 88:109-17. 2010
    ..Site-directed and random mutagenesis analyses suggest that the ATP-bound form of D1 changes an inter-domain interaction, thereby perturbing an essential function of Cdc48p/p97...
  44. ncbi request reprint [Neurodegenerative disease models of AAA proteins in C. elegans]
    Kunitoshi Yamanaka
    Tanpakushitsu Kakusan Koso 49:1124-6. 2004
  45. ncbi request reprint Carboxyl terminal region of the MukB protein in Escherichia coli is essential for DNA binding activity
    A Z Saleh
    Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
    FEMS Microbiol Lett 143:211-6. 1996
    ..This mutant MukB protein was defective for DNA binding, while the ATP binding activity remained unaffected. A truncated MukB protein that is short of 109 amino acids from the C-terminus failed to bind DNA...
  46. pmc E.coli MukB protein involved in chromosome partition forms a homodimer with a rod-and-hinge structure having DNA binding and ATP/GTP binding activities
    H Niki
    Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
    EMBO J 11:5101-9. 1992
    ..Photoaffinity cross-linking experiments showed that MukB binds to ATP and GTP in the presence of Zn2+. Throughout the purification steps, acyl carrier protein was co-purified with MukB...
  47. ncbi request reprint Characterization of translucent segments observed in an smbA mutant of Escherichia coli
    K Yamanaka
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Japan
    FEMS Microbiol Lett 116:61-6. 1994
    ..Electron microscopic observation revealed that the translucent segments resulted from the enlargement of a periplasmic space by separation of the inner membrane from the peptidoglycan layer and the outer membrane...
  48. ncbi request reprint Multicopy suppressors, mssA and mssB, of an smbA mutation of Escherichia coli
    K Yamanaka
    Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
    Mol Gen Genet 243:9-16. 1994
    ..MssA and MssB might also relate to the expression of some of these genes. Multiple copies mssA and mssB suppressed the various phenotypic features of the smbA2 mutant to various extents, suppressing the cold-sensitive growth completely...
  49. ncbi request reprint Identification of a cysteine residue important for the ATPase activity of C. elegans fidgetin homologue
    Yasufumi Yakushiji
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 862 0976, Japan
    FEBS Lett 578:191-7. 2004
    ..These results suggest that the unique position of cysteine 368, located immediately downstream of the Walker A motif, plays an important role in the ATP hydrolysis process of C. elegans F32D1.1 protein...
  50. ncbi request reprint New killing system controlled by two genes located immediately upstream of the mukB gene in Escherichia coli
    J Feng
    Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
    Mol Gen Genet 243:136-47. 1994
    ..It was also demonstrated that KicA and KicB can function as a post-segregational killing system, when the genes are transferred from the E. coli chromosome onto a plasmid...
  51. pmc Identification and characterization of the smbA gene, a suppressor of the mukB null mutant of Escherichia coli
    K Yamanaka
    Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
    J Bacteriol 174:7517-26. 1992
    ..The smbA mutants are sensitive to a detergent, sodium dodecyl sulfate, and they show a novel morphological phenotype under nonpermissive conditions, suggesting a defect in specific membrane sites...
  52. pmc RNase E polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coli
    M Kido
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kumamoto, Japan
    J Bacteriol 178:3917-25. 1996
    ..RNase E and PNPase of the multiprotein complex presumably cooperate for effective processing and turnover of specific substrates, such as mRNAs and other RNAs in vivo...
  53. ncbi request reprint Cloning, sequencing, and characterization of multicopy suppressors of a mukB mutation in Escherichia coli
    K Yamanaka
    Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
    Mol Microbiol 13:301-12. 1994
    ..Hence, the msmB and msmC genes were renamed cspC and cspE, respectively. Possible mechanisms for suppression of the mukB106 mutation are discussed...
  54. ncbi request reprint Identification of the cpdA gene encoding cyclic 3',5'-adenosine monophosphate phosphodiesterase in Escherichia coli
    R Imamura
    Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kumamoto, Kumamoto 862, Japan
    J Biol Chem 271:25423-9. 1996
    ..Our results suggested that regulation of intracellular concentration of cAMP is dependent not only on synthesis of cAMP but also on hydrolysis of cAMP by cAMP phosphodiesterase...
  55. ncbi request reprint Two mutant alleles of mukB, a gene essential for chromosome partition in Escherichia coli
    K Yamanaka
    Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
    FEMS Microbiol Lett 123:27-31. 1994
    ....
  56. ncbi request reprint Characterization of the smtA gene encoding an S-adenosylmethionine-dependent methyltransferase of Escherichia coli
    K Yamanaka
    Department of Molecular Cell Biology, Kumamoto University School of Medicine, Japan
    FEMS Microbiol Lett 133:59-63. 1995
    ..The smtA gene is not essential for cell growth and its expression is positively regulated by H-NS, an Escherichia coli histone-like protein...
  57. ncbi request reprint Crystallization of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli
    Szymon Krzywda
    Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, England
    Acta Crystallogr D Biol Crystallogr 58:1066-7. 2002
    ..The ATPase domain of FtsH from Escherichia coli has been crystallized from ammonium sulfate solutions and crystals diffracting to 1.5 A resolution have been obtained...
  58. ncbi request reprint The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 A resolution
    Szymon Krzywda
    Structural Biology Laboratory, Department of Chemistry, University of York, United Kingdom
    Structure 10:1073-83. 2002
    ..A sulfate anion in the ATP binding pocket mimics the beta-phosphate group of an adenine nucleotide. A hexamer form of FtsH has been modeled, providing insights into possible modes of nucleotide binding and intersubunit catalysis...
  59. ncbi request reprint Allelic characterization of the leaf-variegated mutation var2 identifies the conserved amino acid residues of FtsH that are important for ATP hydrolysis and proteolysis
    Wataru Sakamoto
    Research Institute for Bioresources, Okayama University, 2 20 1 Chuo, Kurashiki, Okayama 710 0046, Japan
    Plant Mol Biol 56:705-16. 2004
    ..Based on these results, we propose that the conserved Gly-Ala-Asp motif plays an important role in FtsH activity. Thus, characterization of the var2 alleles could help to identify the physiologically important domain of FtsH...
  60. ncbi request reprint C. elegans RBX-2-CUL-5- and RBX-1-CUL-2-based complexes are redundant for oogenesis and activation of the MAP kinase MPK-1
    Yohei Sasagawa
    Graduate School of Life Sciences, Tohoku University, 2 1 1 Katahira, Aoba, Sendai, Miyagi, Japan
    FEBS Lett 581:145-50. 2007
    ..Yeast two-hybrid analysis and RNAi-knockdown experiments suggest that oocyte maturation from pachytene exit and MPK-1 activation are redundantly controlled by the RBX-2-CUL-5- and RBX-1-CUL-2-based complexes...