hslV

Summary

Gene Symbol: hslV
Description: peptidase component of the HslUV protease
Alias: ECK3924, JW3903, clpQ, htpO, yiiC
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  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. 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
    ..It is the product of the 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...
  3. Munavar H, Zhou Y, Gottesman S. Analysis of the Escherichia coli Alp phenotype: heat shock induction in ssrA mutants. J Bacteriol. 2005;187:4739-51 pubmed
    ..Thus, ssrA and faa each suppress two lon mutant phenotypes but by somewhat different mechanisms, with heat shock induction playing a major role. ..
  4. Khattar M. Overexpression of the hslVU operon suppresses SOS-mediated inhibition of cell division in Escherichia coli. FEBS Lett. 1997;414:402-4 pubmed
    ..Further 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...
  5. Lau Wong I, Locke T, Ellison M, Raivio T, Frost L. Activation of the Cpx regulon destabilizes the F plasmid transfer activator, TraJ, via the HslVU protease in Escherichia coli. Mol Microbiol. 2008;67:516-27 pubmed
    ..coli C600 cpxA101* background. Double mutants of cpxA101* and hslV or hslU restored TraJ and F conjugation to wild-type levels...
  6. Kanemori M, Yanagi H, Yura T. Marked instability of the sigma(32) heat shock transcription factor at high temperature. Implications for heat shock regulation. J Biol Chem. 1999;274:22002-7 pubmed
  7. 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
    ..Inactivation of the chromosomal copy of clpY or clpQ leads to further stabilization of SulA in a lon mutant but not in lon+ cells...
  8. 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
    ..Six identical subunits of both ClpY and ClpQ self-assemble into an oligomeric ring, and two rings of each subunit, two ClpQ rings surrounded by single ClpY ..
  9. 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...

More Information

Publications70

  1. 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...
  2. 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...
  3. Bochtler M, Ditzel L, Groll M, Huber R. Crystal structure of heat shock locus V (HslV) from Escherichia coli. Proc Natl Acad Sci U S A. 1997;94:6070-4 pubmed
    Heat shock locus V (HslV; also called ClpQ) is the proteolytic core of the ATP-dependent protease HslVU in Escherichia coli. It has sequence similarity with the beta-type subunits of the eukaryotic and archaebacterial proteasomes...
  4. Kuo M, Chen K, Wu W. Regulation of RcsA by the ClpYQ (HslUV) protease in Escherichia coli. Microbiology. 2004;150:437-46 pubmed
    ..This paper shows that overexpression of ClpQ and ClpY suppresses the mucoid phenotype of a lon mutant...
  5. 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...
  6. Lien H, Shy R, Peng S, Wu Y, Weng Y, Chen H, et al. Characterization of the Escherichia coli ClpY (HslU) substrate recognition site in the ClpYQ (HslUV) protease using the yeast two-hybrid system. J Bacteriol. 2009;191:4218-31 pubmed publisher
    In Escherichia coli, ClpYQ (HslUV) is a two-component ATP-dependent protease in which ClpQ is the peptidase subunit and ClpY is the ATPase and the substrate-binding subunit...
  7. Nakasono S, Saiki H. Effect of ELF magnetic fields on protein synthesis in Escherichia coli K12. Radiat Res. 2000;154:208-16 pubmed
    ..in the levels of synthesis of the stress proteins were observed in heat-shocked cells (CH60, CH10, HTPG, DNAK, HSLV, IBPA and some unidentified proteins) and in cells grown under anaerobic conditions (DNAK, PFLB, RECA, USPA and ..
  8. Schmidt R, Bukau B, Mogk A. Principles of general and regulatory proteolysis by AAA+ proteases in Escherichia coli. Res Microbiol. 2009;160:629-36 pubmed publisher
    ..Here we summarize the various strategies that tightly control substrate degradation from both sides: the generation of accessible degrons and their specific recognition by AAA+ proteases and cognate adaptor proteins. ..
  9. 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
    The hslVU operon in Escherichia coli encodes 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...
  10. Sousa M, Kessler B, Overkleeft H, McKay D. Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: corroboration of a proposed mechanism of allosteric activation of HslV by HslU. J Mol Biol. 2002;318:779-85 pubmed publisher
    On the basis of the structure of a HslUV complex, a mechanism of allosteric activation of the HslV protease, wherein binding of the HslU chaperone propagates a conformational change to the active site cleft of the protease, has been ..
  11. Kwon A, Kessler B, Overkleeft H, McKay D. Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome. J Mol Biol. 2003;330:185-95 pubmed
    In the prokaryotic homolog of the eukaryotic proteasome, HslUV, the "double donut" HslV protease is allosterically activated by HslU, an AAA protein of the Clp/Hsp100 family consisting of three (amino-terminal, carboxy-terminal, and ..
  12. Wang J. A second response in correcting the HslV-HslU quaternary structure. J Struct Biol. 2003;141:7-8 pubmed
  13. Ramachandran R, Hartmann C, Song H, Huber R, Bochtler M. Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY). Proc Natl Acad Sci U S A. 2002;99:7396-401 pubmed
    HslVU is a bacterial homolog of the proteasome, where HslV is the protease that is activated by HslU, an ATPase and chaperone...
  14. Liang W, Deutscher M. Transfer-messenger RNA-SmpB protein regulates ribonuclease R turnover by promoting binding of HslUV and Lon proteases. J Biol Chem. 2012;287:33472-9 pubmed publisher
    ..RNase R in stationary phase or in cold-shocked cells is not acetylated, and thereby remains stable. Such a regulatory mechanism, dependent on protein acetylation, has not been observed previously in bacterial cells...
  15. 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...
  16. 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 ..
  17. 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
    ..of Leptospira 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...
  18. 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...
  19. Biran D, Gur E, Gollan L, Ron E. Control of methionine biosynthesis in Escherichia coli by proteolysis. Mol Microbiol. 2000;37:1436-43 pubmed
    ..Alternatively, the proteolytic processing of HTS may be unique to this enzyme and could reflect its central role in regulating bacterial growth, especially at elevated temperatures. ..
  20. Gille C, Goede A, Schl etelburg C, Preissner R, Kloetzel P, G bel U, et al. A comprehensive view on proteasomal sequences: implications for the evolution of the proteasome. J Mol Biol. 2003;326:1437-48 pubmed
    ..tertiary structure: the 20S proteasome and the proteasome-like heat shock protein encoded by heat shock locus V, hslV. Usually, each biological kingdom is characterized by its specific type of proteasome...
  21. 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
    ..HslVU is a two-component ATP-dependent protease composed of the proteasome-related peptidase HslV (beta-subunit) and the ATPase HslU...
  22. 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...
  23. 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
    ClpQ (HslV) is a homolog of the beta-subunits of the 20S proteasome. In E. coli, it is expressed from an operon that also encodes ClpY (HslU), an ATPase homologous to the protease chaperone, ClpX...
  24. 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
    ..hydrolyze ATP or support the ATP-dependent hydrolysis of N-carbobenzoxy-Gly-Gly-Leu-7-amido-4-methyl coumarin by HslV. The wild-type HslU (a mixture of monomer and dimer) formed a multimer containing 6-8 subunits in the presence of ..
  25. Lien H, Yu C, Liou C, Wu W. Regulation of clpQ?Y? (hslV?U?) gene expression in Escherichia coli. Open Microbiol J. 2009;3:29-39 pubmed publisher
    The Escherichia coli ClpYQ (HslUV) complex is an ATP-dependent protease, and the clpQ?Y? (hslV?U?) operon encodes two heat shock proteins, ClpQ and ClpY, respectively...
  26. 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 hexameric HslU ATPase binds the dodecameric HslV peptidase and forms an ATP-dependent HslVU protease. ..
  27. Mizrahi I, Biran D, Ron E. Requirement for the acetyl phosphate pathway in Escherichia coli ATP-dependent proteolysis. Mol Microbiol. 2006;62:201-11 pubmed
    ..In this communication we present evidence for the general role of the acetyl phosphate pathway in protein degradation. ..
  28. Fredriksson A, Nystrom T. Conditional and replicative senescence in Escherichia coli. Curr Opin Microbiol. 2006;9:612-8 pubmed
    ..Thus, bacterial physiology might entail both conditional and mandatory aging processes. ..
  29. Lee J, Park E, Bang O, Eom S, Cheong G, Chung C, et al. Nucleotide triphosphates inhibit the degradation of unfolded proteins by HslV peptidase. Mol Cells. 2007;23:252-7 pubmed
    Escherichia coli HslVU is an ATP-dependent protease consisting of two heat shock proteins, the HslU ATPase and HslV peptidase...
  30. Gage D, Neidhardt F. Adaptation of Escherichia coli to the uncoupler of oxidative phosphorylation 2,4-dinitrophenol. J Bacteriol. 1993;175:7105-8 pubmed
    ..The rates of synthesis of 53 proteins were increased following exposure to 2,4-dinitrophenol. Adaptation was accelerated when the cofactor pyrroloquinoline quinone was provided in the growth medium. ..
  31. 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...
  32. Chuang S, Blattner F. Characterization of twenty-six new heat shock genes of Escherichia coli. J Bacteriol. 1993;175:5242-52 pubmed
    ..Possible assignments of some of the hsl genes to known proteins are discussed. ..
  33. 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. ..
  34. 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 ..
  35. Bochtler M, Hartmann C, Song H, Bourenkov G, Bartunik H, Huber R. The structures of HsIU and the ATP-dependent protease HsIU-HsIV. Nature. 2000;403:800-5 pubmed publisher
    ..Its protease component HslV shares approximately 20% sequence similarity and a conserved fold with 20S proteasome beta-subunits...
  36. Jain R, Chan M. Support for a potential role of E. coli oligopeptidase A in protein degradation. Biochem Biophys Res Commun. 2007;359:486-90 pubmed
    ..Herein, we provide initial support for this hypothesis by demonstrating that OpdA efficiently cleaves the peptides generated by the activity of the three primary ATP-dependent proteases from E. coli-Lon, HslUV, and ClpAP. ..
  37. Park E, Rho Y, Koh O, Ahn S, Seong I, Song J, et al. Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase. J Biol Chem. 2005;280:22892-8 pubmed
    HslVU is an ATP-dependent protease consisting of HslU ATPase and HslV peptidase...
  38. Chang C, Hu H, Tsai C, Wu W. The degradation of RcsA by ClpYQ(HslUV) protease in Escherichia coli. Microbiol Res. 2016;184:42-50 pubmed publisher
    ..the comparative half-life experiments performed in the bacterial strains SG22623 (lon) and AC3112 (lon clpY clpQ) indicated that the RcsA turnover rate in AC3112 was relatively slow and RcsA was stable at 30°C or 41°C...
  39. Hauser R, Ceol A, Rajagopala S, Mosca R, Siszler G, Wermke N, et al. A second-generation protein-protein interaction network of Helicobacter pylori. Mol Cell Proteomics. 2014;13:1318-29 pubmed publisher
    ..coli of which one third turned out to be conserved in both species. ..
  40. Park E, Lee J, Yoo H, Ha B, An J, Jeon Y, et al. Structural alteration in the pore motif of the bacterial 20S proteasome homolog HslV leads to uncontrolled protein degradation. J Mol Biol. 2013;425:2940-54 pubmed publisher
    ..HslVU is a prototype of such enzymes, consisting of the hexameric HslU ATPase and the dodecameric HslV protease. HslV forms a barrel-shaped proteolytic chamber with two constricted axial pores...
  41. 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
    ..b>HtpO heat shock proteins...
  42. 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
    ..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 ..
  43. Fredriksson A, Ballesteros M, Dukan S, Nystrom T. Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon. J Bacteriol. 2005;187:4207-13 pubmed
  44. Nishii W, Takahashi K. Determination of the cleavage sites in SulA, a cell division inhibitor, by the ATP-dependent HslVU protease from Escherichia coli. FEBS Lett. 2003;553:351-4 pubmed
  45. 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...
  46. Wang J, Hartling J, Flanagan J. Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask. J Struct Biol. 1998;124:151-63 pubmed
    ..Comparison of the ClpP structure with those of the 20S proteasome and HslV reveals a striking example of evolutionary convergence, despite them being unrelated in sequence and fold...
  47. 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
    ..HslVU protease, mutagenesis was performed to replace either Cys261 or Cys287 in HslU with Val and Cys159 in HslV with Ser or Ala...
  48. 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
    ..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...
  49. Hsieh F, Chen C, Weng Y, Peng S, Chen Y, Huang L, et al. Stepwise activity of ClpY (HslU) mutants in the processive degradation of Escherichia coli ClpYQ (HslUV) protease substrates. J Bacteriol. 2011;193:5465-76 pubmed publisher
    ..HslUV) is a two-component ATP-dependent protease composed of ClpY (HslU), an ATPase with unfolding activity, and ClpQ (HslV), a peptidase...
  50. Lee J, Park E, Jeong M, Jeon Y, Eom S, Seol J, et al. HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis. J Biol Chem. 2009;284:33475-84 pubmed publisher
    ..protease distantly related to eukaryotic proteasomes consisting of hexameric HslU ATPase and dodecameric HslV protease...
  51. Sousa M, Trame C, Tsuruta H, Wilbanks S, Reddy V, McKay D. Crystal and solution structures of an HslUV protease-chaperone complex. Cell. 2000;103:633-43 pubmed
    HslUV is a "prokaryotic proteasome" composed of the HslV protease and the HslU ATPase, a chaperone of the Clp/Hsp100 family. The 3.4 A crystal structure of an HslUV complex is presented here...
  52. 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
    ..HslU ATPase forms a hexameric ring, and HslV peptidase is a dodecamer consisting of two stacked hexameric rings...
  53. 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...
  54. 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...
  55. Koodathingal P, Jaffe N, Kraut D, Prakash S, Fishbain S, Herman C, et al. ATP-dependent proteases differ substantially in their ability to unfold globular proteins. J Biol Chem. 2009;284:18674-84 pubmed publisher
    ..We propose that these differences in unfolding abilities contribute to the fates of substrate proteins and may act as a further layer of selectivity during protein destruction. ..
  56. Song H, Bochtler M, Azim M, Hartmann C, Huber R, Ramachandran R. Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV. Biophys Chem. 2003;100:437-52 pubmed
    ..It consists of HslV, the protease, and HslU, the ATPase and chaperone...
  57. Kanemori M, Yanagi H, Yura T. The ATP-dependent HslVU/ClpQY protease participates in turnover of cell division inhibitor SulA in Escherichia coli. J Bacteriol. 1999;181:3674-80 pubmed
    ..These results suggest that HslVU as well as Lon participates in the in vivo turnover of SulA and that HslVU becomes essential for growth when the Lon (and Clp) protease level is reduced below a critical threshold. ..
  58. Kanemori M, Nishihara K, Yanagi H, Yura T. Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli. J Bacteriol. 1997;179:7219-25 pubmed
    ..Thus, a set of ATP-dependent proteases appear to play synergistic roles in the negative control of the heat shock response by modulating in vivo turnover of sigma32 as well as through degradation of abnormal proteins. ..
  59. Kwon A, Trame C, McKay D. Kinetics of protein substrate degradation by HslUV. J Struct Biol. 2004;146:141-7 pubmed
    ..Clp/Hsp100 family, binds and unfolds substrates and translocates the polypeptide into the catalytic cavity of the HslV protease...
  60. Bernstein H, Hyndman J. Physiological basis for conservation of the signal recognition particle targeting pathway in Escherichia coli. J Bacteriol. 2001;183:2187-97 pubmed
    ..By contrast, the heat shock-regulated proteases Lon and ClpQ became essential for viability when SRP levels were reduced...
  61. 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...