hslU

Summary

Gene Symbol: hslU
Description: ATP-dependent protease ATP-binding protein HslU
Species: Escherichia coli O157:H7 str. Sakai

Top Publications

  1. Gottesman S, Clark W, De Crecy Lagard V, Maurizi M. ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities. J Biol Chem. 1993;268:22618-26 pubmed
    ..It appears that selectivity of degradation by ClpP in vivo is determined by interaction of ClpP with different regulatory ATPase subunits. ..
  2. Karata K, Verma C, Wilkinson A, Ogura T. Probing the mechanism of ATP hydrolysis and substrate translocation in the AAA protease FtsH by modelling and mutagenesis. Mol Microbiol. 2001;39:890-903 pubmed
    ..Furthermore, comparative structural analysis of FtsH and a related ATPase, HslU, reveals interesting similarities and differences in mechanism.
  3. Seong I, Oh J, Lee J, Tanaka K, Chung C. The HslU ATPase acts as a molecular chaperone in prevention of aggregation of SulA, an inhibitor of cell division in Escherichia coli. FEBS Lett. 2000;477:224-9 pubmed
    HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase. SulA, which is an inhibitor of cell division and has high tendency of aggregation, is degraded by HslVU protease...
  4. Bogyo M, McMaster J, Gaczynska M, Tortorella D, Goldberg A, Ploegh H. Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors. Proc Natl Acad Sci U S A. 1997;94:6629-34 pubmed
    ..125I-NIP-L3VS covalently modifies the HslV subunit of the Escherichia coli protease complex HslV/HslU, a reaction that requires ATP, and supports a catalytic mechanism shared with that of the eukaryotic proteasome.
  5. Becker J, Brendel M. Molecular characterization of the xerC gene of Lactobacillus leichmannii encoding a site-specific recombinase and two adjacent heat shock genes. Curr Microbiol. 1996;32:232-6 pubmed
    ..of the complete ORFs showed considerable similarities with the already known sequences of the xerC, hslV, and hslU gene products of Escherichia coli: the site-specific XerC recombinase, a member of the lambda integrase family, and ..
  6. Khattar M. Overexpression of the hslVU operon suppresses SOS-mediated inhibition of cell division in Escherichia coli. FEBS Lett. 1997;414:402-4 pubmed
    ..characterisation of pHL1 revealed that resistance to nitrofurantoin was due to the overexpression of the hslV-hslU operon which encodes an ATP-dependent protease complex in E. coli...
  7. Rohrwild M, Pfeifer G, Santarius U, Muller S, Huang H, Engel A, et al. The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome. Nat Struct Biol. 1997;4:133-9 pubmed
    ..We have used electron microscopy and image analysis to examine the structural organization of HslV and HslU homo-oligomers and the active HslVU enzyme...
  8. Rohrwild M, Coux O, Huang H, Moerschell R, Yoo S, Seol J, et al. HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome. Proc Natl Acad Sci U S A. 1996;93:5808-13 pubmed
    ..heat-shock locus hslVU that encodes two proteins: HslV, a 19-kDa protein similar to proteasome beta subunits, and HslU, a 50-kDa protein related to the ATPase ClpX...
  9. Katayama T, Kubota T, Takata M, Akimitsu N, Sekimizu K. Disruption of the hslU gene, which encodes an ATPase subunit of the eukaryotic 26S proteasome homolog in Escherichia coli, suppresses the temperature-sensitive dnaA46 mutation. Biochem Biophys Res Commun. 1996;229:219-24 pubmed
    ..We found that the hslU gene is required for the temperature (40 degrees C)-sensitive phenotype of the dnaA46 mutant, while other soluble ..

More Information

Publications37

  1. Seong I, Oh J, Yoo S, Seol J, Chung C. ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli. FEBS Lett. 1999;456:211-4 pubmed
    HslVU is an ATP-dependent protease consisting of two multimeric components, the HslU ATPase and the HslV peptidase...
  2. Lee Y, Chang C, Kuo C, Chen M, Yu C, Lin P, et al. Subunit oligomerization and substrate recognition of the Escherichia coli ClpYQ (HslUV) protease implicated by in vivo protein-protein interactions in the yeast two-hybrid system. J Bacteriol. 2003;185:2393-401 pubmed
    ..Thus, we demonstrated in vivo hetero- and homointeractions of ClpQ and ClpY molecules, as well as a direct association between ClpY and substrate SulA, thereby supporting previous in vitro biochemical findings...
  3. Lin M, Li Y. PCR genome walking identifies a genetic locus comprising two heat shock genes (hslV and hslU) from Leptospira borgpetersenii serovar hardjobovis. Curr Microbiol. 2001;43:452-6 pubmed
    ..borgpetersenii serovar hardjobovis has identified a genetic locus comprising two heat shock genes (hslV and hslU). This is the first molecular study on hslV and hslU in a Leptospira species...
  4. Song H, Hartmann C, Ramachandran R, Bochtler M, Behrendt R, Moroder L, et al. Mutational studies on HslU and its docking mode with HslV. Proc Natl Acad Sci U S A. 2000;97:14103-8 pubmed publisher
    ..Despite detailed crystal and molecular structure determinations of free HslV and HslU, the mechanism of ATP-dependent peptide and protein hydrolysis remained unclear, mainly because the productive ..
  5. Huang H, Goldberg A. Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis. J Biol Chem. 1997;272:21364-72 pubmed
    HslVU is a new Escherichia coli ATP-dependent protease composed of two multimeric complexes: the HslU ATPase and the HslV peptidase. Prior studies indicated that HslVU requires ATP hydrolysis for the cleavage of peptides and proteins...
  6. Wang J, Song J, Franklin M, Kamtekar S, Im Y, Rho S, et al. Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism. Structure. 2001;9:177-84 pubmed
    The bacterial heat shock locus HslU ATPase and HslV peptidase together form an ATP-dependent HslVU protease. Bacterial HslVU is a homolog of the eukaryotic 26S proteasome...
  7. Missiakas D, Schwager F, Betton J, Georgopoulos C, Raina S. Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli. EMBO J. 1996;15:6899-909 pubmed
    ..One such locus was identified and shown to carry the recently sequenced hslV hslU (clpQ clpY) operon...
  8. Wang J. A corrected quaternary arrangement of the peptidase HslV and atpase HslU in a cocrystal structure. J Struct Biol. 2001;134:15-24 pubmed
    The bacterial heat shock locus HslU ATPase and HslV peptidase together form an ATP-dependent HslVU protease...
  9. Yoo S, Kim H, Shin D, Lee C, Seong I, Seol J, et al. Effects of the cys mutations on structure and function of the ATP-dependent HslVU protease in Escherichia coli. The Cys287 to Val mutation in HslU uncouples the ATP-dependent proteolysis by HslvU from ATP hydrolysis. J Biol Chem. 1998;273:22929-35 pubmed
    ..Cys residues in the ATP-dependent HslVU protease, mutagenesis was performed to replace either Cys261 or Cys287 in HslU with Val and Cys159 in HslV with Ser or Ala...
  10. Couvreur B, Wattiez R, Bollen A, Falmagne P, Le Ray D, Dujardin J. Eubacterial HslV and HslU subunits homologs in primordial eukaryotes. Mol Biol Evol. 2002;19:2110-7 pubmed publisher
    ..We showed that genes homologous to eubacterial HslV (ClpQ) and HslU (ClpY) are present in the genome of trypanosomatid protozoa and are expressed...
  11. Seol J, Yoo S, Shin D, Shim Y, Kang M, Goldberg A, et al. The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase. Eur J Biochem. 1997;247:1143-50 pubmed
    HslVU in Escherichia coli a new two-component ATP-dependent protease composed of two heat-shock proteins, the HslU ATPase and the HslV peptidase which is related to proteasome beta-type subunits...
  12. Chuang S, Burland V, Plunkett G, Daniels D, Blattner F. Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli. Gene. 1993;134:1-6 pubmed
    ..Located at 88.9 min, the hslVU operon specifies proteins of 19.1 kDa (HslV) and 49.6 kDa (HslU). Multiple tsp were found in this operon...
  13. Slominska M, Wahl A, Wegrzyn G, Skarstad K. Degradation of mutant initiator protein DnaA204 by proteases ClpP, ClpQ and Lon is prevented when DNA is SeqA-free. Biochem J. 2003;370:867-71 pubmed
    ..Its cognate protease ClpQ, as well as Lon protease, degraded DnaA204 to the same degree as ClpP. The chaperones GroES, GroEL and DnaK contributed to stabilization of DnaA204 protein. ..
  14. Yoo S, Seol J, Kang M, Chung C. Poly-L-lysine activates both peptide and ATP hydrolysis by the ATP-dependent HslVU protease in Escherichia coli. Biochem Biophys Res Commun. 1996;229:531-5 pubmed
    Hs1VU in E. coli is a new type of ATP-dependent protease composed of two heat shock proteins, the HslU ATPase and the HslV peptidase related to certain beta-type subunits of the 20S proteasome...
  15. Goldberg A, Akopian T, Kisselev A, Lee D, Rohrwild M. New insights into the mechanisms and importance of the proteasome in intracellular protein degradation. Biol Chem. 1997;378:131-40 pubmed
    ..ATP-dependent protease composed of the proteasome-related peptidase HslV (beta-subunit) and the ATPase HslU. In active HslVU complex, cleavage of small peptides and proteins requires the presence of ATP...
  16. Shin D, Yoo S, Shim Y, Seol J, Kang M, Chung C. Mutational analysis of the ATP-binding site in HslU, the ATPase component of HslVU protease in Escherichia coli. FEBS Lett. 1996;398:151-4 pubmed
    b>HslU is the ATPase component of the ATP-dependent HslVU protease in Escherichia coli...
  17. Yoo S, Seol J, Shin D, Rohrwild M, Kang M, Tanaka K, et al. Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli. J Biol Chem. 1996;271:14035-40 pubmed
    ..two heat shock proteins, HslV, a 19-kDa protein homologous to beta-type subunits of the 20 S proteasomes, and HslU, a 50-kDa protein related to the ATPase ClpX...
  18. Smith C, Baker T, Sauer R. Lon and Clp family proteases and chaperones share homologous substrate-recognition domains. Proc Natl Acad Sci U S A. 1999;96:6678-82 pubmed
  19. Yoo S, Seol J, Seong I, Kang M, Chung C. ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli. Biochem Biophys Res Commun. 1997;238:581-5 pubmed
    HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase...
  20. Kang M, Lim B, Seong I, Seol J, Tanahashi N, Tanaka K, et al. The ATP-dependent CodWX (HslVU) protease in Bacillus subtilis is an N-terminal serine protease. EMBO J. 2001;20:734-42 pubmed
    HslVU is a two-component ATP-dependent protease, consisting of HslV peptidase and HslU ATPase...
  21. Wang J, Song J, Seong I, Franklin M, Kamtekar S, Eom S, et al. Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU. Structure. 2001;9:1107-16 pubmed
    The bacterial heat shock locus ATPase HslU is an AAA(+) protein that has structures known in many nucleotide-free and -bound states. Nucleotide is required for the formation of the biologically active HslU hexameric assembly...
  22. Wu W, Zhou Y, Gottesman S. Redundant in vivo proteolytic activities of Escherichia coli Lon and the ClpYQ (HslUV) protease. J Bacteriol. 1999;181:3681-7 pubmed
    ..Thus, a protease with a structure and an active site different from those of Lon is capable of recognizing and degrading two different Lon substrates and appears to act as a backup for Lon under certain conditions. ..
  23. Peruski L, Neidhardt F. Identification of a conditionally essential heat shock protein in Escherichia coli. Biochim Biophys Acta. 1994;1207:165-72 pubmed
    ..5 is nearly constitutive, increasing slightly with growth rate in media of different composition, and (iii) this protein is essential for growth at high temperature. ..
  24. Kessel M, Wu W, Gottesman S, Kocsis E, Steven A, Maurizi M. Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY. FEBS Lett. 1996;398:274-8 pubmed
    ..In E. coli, it is expressed from an operon that also encodes ClpY (HslU), an ATPase homologous to the protease chaperone, ClpX...
  25. Bochtler M, Song H, Hartmann C, Ramachandran R, Huber R. The quaternary arrangement of HslU and HslV in a cocrystal: a response to Wang, Yale. J Struct Biol. 2001;135:281-93 pubmed
    Protease HslV and ATPase HslU form an ATP-dependent protease in bacteria. We have previously determined the structure of the components of this protease...
  26. Wang J. A second response in correcting the HslV-HslU quaternary structure. J Struct Biol. 2003;141:7-8 pubmed
  27. Seong I, Kang M, Choi M, Lee J, Koh O, Wang J, et al. The C-terminal tails of HslU ATPase act as a molecular switch for activation of HslV peptidase. J Biol Chem. 2002;277:25976-82 pubmed publisher
    The bacterial HslVU ATP-dependent protease is a homolog of the eukaryotic 26 S proteasome. HslU ATPase forms a hexameric ring, and HslV peptidase is a dodecamer consisting of two stacked hexameric rings...
  28. Yoo S, Shim Y, Seong I, Seol J, Kang M, Chung C. Mutagenesis of two N-terminal Thr and five Ser residues in HslV, the proteolytic component of the ATP-dependent HslVU protease. FEBS Lett. 1997;412:57-60 pubmed
    HslVU in E. coli is a new type of ATP-dependent protease consisting of two heat shock proteins: the HslU ATPase and the HslV peptidase that has two repeated Thr residues at its N terminus, like certain beta-type subunit of the 20S ..