hslU

Summary

Gene Symbol: hslU
Description: molecular chaperone and ATPase component of HslUV protease
Alias: ECK3923, JW3902, clpY, htpI
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. 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...
  2. 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
  3. 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 ..
  4. 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...
  5. 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...
  6. 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...
  7. 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...
  8. 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...
  9. 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...

More Information

Publications72

  1. 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
    ..Fragments corresponding to these sequences are stably and independently folded for Lon, ClpA, and ClpY. The corresponding regions from ClpB and ClpX are unstable...
  2. 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
    ..The suppression of UV sensitivity, both in the original Alp strain and in faa mutants, is reversed by mutations in clpY, encoding a subunit of the heat shock-induced ClpYQ protease that is known to degrade SulA...
  3. 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...
  4. 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. ..
  5. 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...
  6. 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...
  7. 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...
  8. 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...
  9. 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...
  10. 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...
  11. Shimuta T, Nakano K, Yamaguchi Y, Ozaki S, Fujimitsu K, Matsunaga C, et al. Novel heat shock protein HspQ stimulates the degradation of mutant DnaA protein in Escherichia coli. Genes Cells. 2004;9:1151-66 pubmed
    ..Heat-shock induced proteases such as Clp contain homomultimers of subunit proteins. We propose that HspQ is a new factor involved in the quality control of proteins and that it functions by excluding denatured proteins. ..
  12. Baytshtok V, Chen J, Glynn S, Nager A, Grant R, Baker T, et al. Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation. J Biol Chem. 2017;292:5695-5704 pubmed publisher
    The HslUV proteolytic machine consists of HslV, a double-ring self-compartmentalized peptidase, and one or two AAA+ HslU ring hexamers that hydrolyze ATP to power the unfolding of protein substrates and their translocation into the ..
  13. 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...
  14. 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...
  15. 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
    In Escherichia coli, ClpYQ (HslUV) is a two-component ATP-dependent protease composed of ClpY (HslU), an ATPase with unfolding activity, and ClpQ (HslV), a peptidase...
  16. 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. ..
  17. 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 ..
  18. 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 ..
  19. 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...
  20. 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.
  21. 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
  22. 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. ..
  23. 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
    ..b>HslU is a member of the Hsp100 (Clp) family of ATPases...
  24. 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
    HslVU is a bacterial ATP-dependent protease distantly related to eukaryotic proteasomes consisting of hexameric HslU ATPase and dodecameric HslV protease...
  25. 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
    ..The dnaA204 mutant was not viable in the absence of ClpY, indicating that this chaperone is essential for DnaA204 stability or function...
  26. 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
  27. 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. ..
  28. 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. ..
  29. Peruski L, Neidhardt F. Identification of a conditionally essential heat shock protein in Escherichia coli. Biochim Biophys Acta. 1994;1207:165-72 pubmed
    ..Physiological and genetic analysis demonstrated that (i) the structural gene for this protein, designated htpI, is a member of the sigma 32-dependent heat shock regulon, (ii) at 37 degrees C the synthesis of protein D48...
  30. 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...
  31. 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.
  32. Sundar S, Baker T, Sauer R. The I domain of the AAA+ HslUV protease coordinates substrate binding, ATP hydrolysis, and protein degradation. Protein Sci. 2012;21:188-98 pubmed publisher
    In the AAA+ HslUV protease, substrates are bound and unfolded by a ring hexamer of HslU, before translocation through an axial pore and into the HslV degradation chamber...
  33. 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. ..
  34. 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...
  35. Kask L, Larsson K, Bjellqvist B. Elimination of basic gaps at high pH values in 2-DE. Proteomics. 2009;9:5558-61 pubmed publisher
    ..The use of 8 M urea or thiourea/urea solutions in the electrode wick enables overnight focusing without the appearance of gaps. ..
  36. 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. ..
  37. 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...
  38. 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
    ..complex is an ATP-dependent protease, and the clpQ?Y? (hslV?U?) operon encodes two heat shock proteins, ClpQ and ClpY, respectively...
  39. 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...
  40. 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...
  41. Burton R, Baker T, Sauer R. Nucleotide-dependent substrate recognition by the AAA+ HslUV protease. Nat Struct Mol Biol. 2005;12:245-51 pubmed publisher
    ATP-dependent protein degradation is controlled principally by substrate recognition. The AAA+ HslU ATPase is thought to bind protein substrates, denature them, and translocate the unfolded polypeptide into the HslV peptidase...
  42. 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. ..
  43. 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 ..
  44. 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...
  45. 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...
  46. Wang J. A second response in correcting the HslV-HslU quaternary structure. J Struct Biol. 2003;141:7-8 pubmed
  47. 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...
  48. 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...
  49. Peruski L. Expression of heat shock protein D 48.5 of Escherichia coli is subject to modulation by catabolite repression. Microbiol Res. 1996;151:273-80 pubmed
    ..The lacZ fusion in the structural gene for protein D 48.5 should prove useful as a reporter mechanism to probe the physiology and regulation of the heat shock response. ..
  50. 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. ..
  51. 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...
  52. 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 ..
  53. 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
    ..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 intermediate) ..
  54. 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...
  55. 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...
  56. 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...
  57. 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
    ..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...
  58. 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...
  59. 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...
  60. 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
    ..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 proposed...
  61. 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...
  62. 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
    ..A third group of proteins, ClpY, closely related to ClpX, has been identified by sequence homology...
  63. 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...