Escherichia coli K-12 substr. MG1655 Protein: HslV hexamer

Gene: hslV Accession Numbers: EG11676 (EcoCyc), b3932, ECK3924

Synonyms: yiiC, clpQ, htpO

Regulation Summary Diagram

Regulation summary diagram for hslV

Component of: HslVU protease (extended summary available)

Subunit composition of HslV hexamer = [HslV]6
         peptidase component of the HslVU protease = HslV

HslV is the peptidase component of the HslVU protease, which is composed of HslU and HslV [Rohrwild96, Yoo96]. This ATP-stimulated protease exhibits activity similar to that of the chymotrypsin-like activity of the eukaryotic proteasome [Rohrwild96]. HslV exhibits weak peptidase activity in the absence of HslU [Seol97, Yoo96]. HslV alone hydrolyzed tested proteins at approximately 5% of the rate observed in the presence of HslU [Seol97]. HslV alone can degrade some, but not all, unfolded proteins at varying rates [Lee07c].

The HslVU protease plays a role in clearing the defective peptides produced in the presence of puromycin [Missiakas96a]. HslVU is capable of filling the role of the Lon protease under some conditions [Wu99]. HslVU degrades the Lon substrate SulA [Seong99] and exhibits activity toward DnaA204 mutant protein [Slominska03].

Crystal structures of HslV [Bochtler97] and of the HslVU complex are presented [Bochtler00, Sousa00, Song00, Wang01a, Wang01d, Bochtler01, Wang03a, Kwon03]. HslU and HslV form ring shaped complexes [Rohrwild96] of protein hexamers [Kessel96] that stack into a four-ring cylinder with HslU rings on each end and HslV rings in the center [Rohrwild97]. HslU and HslV co-immunoprecipitate, whereas the association is labile under chromatographic conditions [Rohrwild96]. Interactions among HslU and HslV are discussed in detail [Yoo96, Yoo97, Huang97, Yoo96, Rohrwild97, Song00, Seong02, Lee03, Kwon03, Azim07]. The role of ATP binding and hydrolysis in complex formation and activity is discussed [Yoo96, Yoo97a, Shin96, Huang97, Rohrwild96, Yoo96, Seong99, Song00, Wang01]. Stimulation of HslU-mediated ATP hydrolysis by poly-L-lysine stimulates the peptidase activity of HslV within the HslVU complex [Yoo96a]. The presence of a protein substrate also stimulates HslVU protease activity [Seol97]. The activity of the HslVU complex is discussed in detail [Bogyo97, Huang97, Wang01a, Wang98d]. HslV is modified by an inhibitor of cysteine proteases [Bogyo97].

Mutagenesis studies of HslV have identified the catalytic threonine residue and have identified residues involved in HslU interaction [Yoo97]. A C159S or C159A mutation eliminates peptidase activity, disrupts association with HslU, and inhibits N-ethylmaleimide-mediated dissociation of HslV complexes [Yoo98]. Overproduction of HslU and HslV causes resistance to nitrofurantoin and to UV irradiation in a lon mutant background [Khattar97]. Genetic interactions between hslVU and lon are discussed; Lon functions can be carried out by HslVU [Wu99].

Site-directed mutagenesis of the pore motif of HslV affected the activities of both HslV and HslVU suggesting that the pores have a gating function in substrate degradation. This was supported by the crystal structure of a L88A pore mutant of HslV [Park13]. HslV uses its N-terminal threonine as the active site residue. Mutagenesis studies showed that in the HslV dodecamer only approximately six of the twelve active site threonines are necessary to support full catalytic activity and to stabilize the interaction between HslV and HslU [Lee09g, Park08a]. ATP inhibits the activity of the HslV dodecamer via interaction with the basic apical pore region [Lee07c].

Using methyl-TROSY NMR spectroscopy and site-directed mutagenesis, an allosteric pathway of structural changes in the HslV dodecamer was defined that regulates its proteolytic activity via a dynamic coupling between residues involved in HslU and substrate binding and HslV active site residues [Shi14].

The absence of HslVU homologs in humans and its presence in microbial pathogens makes it a possible drug target. In silico screening of small molecules capable of activating HslV alone identified non-peptide allosteric activators of HslV hydrolytic activity. Their activation ability was confirmed experimentally [Rashid12].

Regulation has been described [Chuang93, Peruski94, Nakasono00]. Transcription [Chuang93, Peruski94] and protein abundance [Nakasono00] are induced by heat shock.

Reviews: [Schmidt09a, Goldberg97]

Locations: cytosol

Map Position: [4,119,780 <- 4,120,310] (88.79 centisomes, 320°)
Length: 531 bp / 176 aa

Molecular Weight of Polypeptide: 19.093 kD (from nucleotide sequence)

Molecular Weight of Multimer: 220 kD (experimental) [Kessel96], 250 kD (experimental) [Yoo96]

Unification Links: ASAP:ABE-0012845, CGSC:34160, DIP:DIP-35866N, EchoBASE:EB1627, EcoGene:EG11676, EcoliWiki:b3932, Mint:MINT-1218940, OU-Microarray:b3932, PortEco:hslV, PR:PRO_000022935, Pride:P0A7B8, Protein Model Portal:P0A7B8, RefSeq:NP_418367, RegulonDB:EG11676, SMR:P0A7B8, String:511145.b3932, UniProt:P0A7B8

Relationship Links: InterPro:IN-FAMILY:IPR001353, InterPro:IN-FAMILY:IPR022281, InterPro:IN-FAMILY:IPR023333, InterPro:IN-FAMILY:IPR029055, PDB:Structure:1E94, PDB:Structure:1G4A, PDB:Structure:1G4B, PDB:Structure:1HQY, PDB:Structure:1HT1, PDB:Structure:1HT2, PDB:Structure:1NED, PDB:Structure:4G4E, Pfam:IN-FAMILY:PF00227, Prosite:IN-FAMILY:PS51476

Gene-Reaction Schematic

Gene-Reaction Schematic

GO Terms:
Biological Process:
Inferred from experimentGO:0009408 - response to heat [Chuang93a]
Inferred from experimentInferred by computational analysisGO:0051603 - proteolysis involved in cellular protein catabolic process [GOA01a, Missiakas96a]
Inferred by computational analysisGO:0006508 - proteolysis [UniProtGOA11, GOA01a]
Inferred by computational analysisGO:0008152 - metabolic process [UniProtGOA11]
Inferred by computational analysisGO:0030163 - protein catabolic process [GOA06]
Molecular Function:
Inferred from experimentInferred by computational analysisGO:0004298 - threonine-type endopeptidase activity [UniProtGOA11, GOA01a, Yoo97]
Inferred from experimentGO:0005515 - protein binding [Lien09, Butland05, Lee03, Wang01, Wang01a]
Inferred from experimentGO:0042802 - identical protein binding [Hauser14, Lasserre06, Lee03]
Inferred by computational analysisGO:0003824 - catalytic activity [UniProtGOA11]
Inferred by computational analysisGO:0008233 - peptidase activity [UniProtGOA11, GOA06]
Inferred by computational analysisGO:0016787 - hydrolase activity [UniProtGOA11]
Inferred by computational analysisGO:0046872 - metal ion binding [UniProtGOA11]
Cellular Component:
Inferred from experimentInferred by computational analysisGO:0005829 - cytosol [DiazMejia09, Ishihama08, Lasserre06]
Inferred from experimentInferred by computational analysisGO:0009376 - HslUV protease complex [GOA06, GOA01a, Rohrwild96, Yoo96]
Inferred by computational analysisGO:0005737 - cytoplasm [UniProtGOA11a, UniProtGOA11]
Inferred by computational analysisGO:0005839 - proteasome core complex [GOA01a]

MultiFun Terms: cell processescell division
information transferprotein relatedchaperoning, repair (refolding)
information transferprotein relatedturnover, degradation
metabolismdegradation of macromoleculesproteins/peptides/glycopeptides
regulationtype of regulationposttranscriptionalproteases, cleavage of compounds

Essentiality data for hslV knockouts:

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enrichedYes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB LennoxYes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerolYes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucoseYes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Last-Curated 06-Aug-2015 by Fulcher C, SRI International

Subunit of: HslVU protease

Synonyms: ClpYQ protease, HslUV protease

Subunit composition of HslVU protease = [(HslU)6]2[(HslV)6]2
         HslU hexamer = (HslU)6 (extended summary available)
                 ATPase component of the HslVU protease = HslU
         HslV hexamer = (HslV)6 (extended summary available)
                 peptidase component of the HslVU protease = HslV

The HslVU protease exhibits ATP-stimulated activity similar to that of the chymotrypsin-like activity of the eukaryotic proteasome [Rohrwild96, RuizGonzalez06].

HslU and HslV form ring shaped complexes [Rohrwild96] of protein hexamers [Kessel96] that stack into a four-ring cylinder with HslU rings on each end and HslV rings in the center [Rohrwild97].

Of the six potential ATP binding sites on an HslU hexamer only three or four molecules of ATP are bound at saturation. ATP binding controls the assembly and activity of the HslVU complex. The binding of a single molecule of ATP to HslU allows it to bind HslV, and binding of additional ATP molecules support substrate recognition and activate ATP hydrolysis which drives substrate unfolding and translocation. This thermodynamic hierarchy ensures efficient function of HslVU [Yakamavich08].

HslV uses its N-terminal threonine as the active site residue. Mutagenesis studies showed that in the HslV dodecamer only approximately six of the twelve active site threonines are necessary to support full catalytic activity and to stabilize the interaction between HslV and HslU [Lee09g].

The HslU hexamer portion of the HslVU complex recognizes and unfolds native protein substrates and then translocates them to the HslV peptidase chamber for degradation. Sequence signals in the substrate are involved in recognition and degradation. A model was proposed that involves tethering of the N- or C-terminus of a substrate to the protease, with the other terminus undergoing translocation and unfolding in the HslU pore [Sundar10].

The HslVU and Lon proteases degrade RNase R in exponential, but not stationary phase cells and tmRNA-SmpB stimulates the process [Liang12]. The F plasmid transfer activator TraJ is degraded by HslVU during extracytoplasmic stress mediated by CpxAR [LauWong08].

HslUV is one of five ATP-dependent proteases in E. coli that are involved in cellular protein quality control. Along with ClpAP, ClpXP, Lon, and FtsH they remove both misfolded and properly folded proteins [Miller13b].

Review: [Sauer04]

Molecular Weight: 820 kD (experimental) [Bochtler00]

Enzymatic reaction of: ATP-dependent HslVU protease

Inferred from experiment

EC Number: 3.4.21.-

a protein + H2O → a peptide + a peptide

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Sequence Features

Protein sequence of peptidase component of the HslVU protease with features indicated

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
Author statement[UniProt15]
UniProt: Removed.
Mutagenesis-Variant 2
Inferred from experiment[Yoo97]
Inferred from experiment[Yoo97]
T → S: 80% reduced protease activity in the absence of HslU. Almost no effect in the presence of HslU.
T → V: No protease activity.
Active-Site 2
Inferred from experiment[Yoo97]
Chain 2 -> 176
Author statement[UniProt15]
UniProt: ATP-dependent protease subunit HslV.
Mutagenesis-Variant 3
Inferred from experiment[Yoo97]
T → S or V: 80% reduced protease activity.
Mutagenesis-Variant 6
Inferred from experiment[Yoo97]
UniProt: No effect.
Mutagenesis-Variant 104
Inferred from experiment[Yoo97]
UniProt: 50% reduced protease activity.
Mutagenesis-Variant 125
Inferred from experiment[Yoo97]
UniProt: Almost no protease activity.
Mutagenesis-Variant 144
Inferred from experiment[Yoo97]
UniProt: No effect.
Metal-Binding-Site 157
Author statement[UniProt15]
UniProt: Sodium; via carbonyl oxygen.
Mutagenesis-Variant 160
Inferred from experiment[Yoo98]
C → A or S: No protease activity. Cannot form complexes with HslU.
Metal-Binding-Site 160
Author statement[UniProt15]
UniProt: Sodium; via carbonyl oxygen.
Metal-Binding-Site 163
Author statement[UniProt15]
UniProt: Sodium; via carbonyl oxygen.
Mutagenesis-Variant 173
Inferred from experiment[Yoo97]
UniProt: Almost no protease activity.

Sequence Pfam Features

Protein sequence of peptidase component of the HslVU protease with features indicated

Feature Class Location Citations Comment
Pfam PF00227 2 -> 167
Inferred by computational analysis[Finn14]
Proteasome : Proteasome subunit

Gene Local Context (not to scale -- see Genome Browser for correct scale)

Gene local context diagram

Transcription Unit

Transcription-unit diagram


10/20/97 Gene b3932 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11676; confirmed by SwissProt match.


Azim07: Azim MK, Noor S (2007). "Characterization of protomer interfaces in HslV protease; the bacterial homologue of 20S proteasome." Protein J 26(4);213-9. PMID: 17522969

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bochtler00: Bochtler M, Hartmann C, Song HK, Bourenkov GP, Bartunik HD, Huber R (2000). "The structures of HsIU and the ATP-dependent protease HsIU-HsIV." Nature 403(6771);800-5. PMID: 10693812

Bochtler01: Bochtler M, Song HK, Hartmann C, Ramachandran R, Huber R (2001). "The quaternary arrangement of HslU and HslV in a cocrystal: a response to Wang, Yale." J Struct Biol 135(3);281-93. PMID: 11722168

Bochtler97: Bochtler M, Ditzel L, Groll M, Huber R (1997). "Crystal structure of heat shock locus V (HslV) from Escherichia coli." Proc Natl Acad Sci U S A 94(12);6070-4. PMID: 9177170

Bogyo97: Bogyo M, McMaster JS, Gaczynska M, Tortorella D, Goldberg AL, Ploegh H (1997). "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 94(13);6629-34. PMID: 9192616

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Chuang93: Chuang SE, Burland V, Plunkett G, Daniels DL, Blattner FR (1993). "Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli." Gene 1993;134(1);1-6. PMID: 8244018

Chuang93a: Chuang SE, Blattner FR (1993). "Characterization of twenty-six new heat shock genes of Escherichia coli." J Bacteriol 175(16);5242-52. PMID: 8349564

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Goldberg97: Goldberg AL, Akopian TN, Kisselev AF, Lee DH, Rohrwild M (1997). "New insights into the mechanisms and importance of the proteasome in intracellular protein degradation." Biol Chem 378(3-4);131-40. PMID: 9165063

Hauser14: Hauser R, Ceol A, Rajagopala SV, Mosca R, Siszler G, Wermke N, Sikorski P, Schwarz F, Schick M, Wuchty S, Aloy P, Uetz P (2014). "A Second-generation Protein-Protein Interaction Network of Helicobacter pylori." Mol Cell Proteomics 13(5);1318-29. PMID: 24627523

Huang97: Huang H, Goldberg AL (1997). "Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis." J Biol Chem 272(34);21364-72. PMID: 9261150

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kessel96: Kessel M, Wu W, Gottesman S, Kocsis E, Steven AC, Maurizi MR (1996). "Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY." FEBS Lett 398(2-3);274-8. PMID: 8977122

Khattar97: Khattar MM (1997). "Overexpression of the hslVU operon suppresses SOS-mediated inhibition of cell division in Escherichia coli." FEBS Lett 414(2);402-4. PMID: 9315728

Kwon: Kwon AR, Trame CB, McKay DB "Kinetics of protein substrate degradation by HslUV." J Struct Biol 146(1-2);141-7. PMID: 15037245

Kwon03: Kwon AR, Kessler BM, Overkleeft HS, McKay DB (2003). "Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome." J Mol Biol 330(2);185-95. PMID: 12823960

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

LauWong08: Lau-Wong IC, Locke T, Ellison MJ, Raivio TL, Frost LS (2008). "Activation of the Cpx regulon destabilizes the F plasmid transfer activator, TraJ, via the HslVU protease in Escherichia coli." Mol Microbiol 67(3);516-27. PMID: 18069965

Lee03: Lee YY, Chang CF, Kuo CL, Chen MC, Yu CH, Lin PI, Wu WF (2003). "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 185(8);2393-401. PMID: 12670962

Lee07c: Lee JW, Park E, Bang O, Eom SH, Cheong GW, Chung CH, Seol JH (2007). "Nucleotide triphosphates inhibit the degradation of unfolded proteins by HslV peptidase." Mol Cells 23(2);252-7. PMID: 17464204

Lee09g: Lee JW, Park E, Jeong MS, Jeon YJ, Eom SH, Seol JH, Chung CH (2009). "HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis." J Biol Chem 284(48);33475-84. PMID: 19801685

Liang12: Liang W, Deutscher MP (2012). "Transfer-messenger RNA-SmpB protein regulates ribonuclease R turnover by promoting binding of HslUV and Lon proteases." J Biol Chem 287(40);33472-9. PMID: 22879590

Lien09: Lien HY, Shy RS, Peng SS, Wu YL, Weng YT, Chen HH, Su PC, Ng WF, Chen YC, Chang PY, Wu WF (2009). "Characterization of the Escherichia coli ClpY (HslU) substrate recognition site in the ClpYQ (HslUV) protease using the yeast two-hybrid system." J Bacteriol 191(13);4218-31. PMID: 19395483

Miller13b: Miller JM, Lin J, Li T, Lucius AL (2013). "E. coli ClpA catalyzed polypeptide translocation is allosterically controlled by the protease ClpP." J Mol Biol 425(15);2795-812. PMID: 23639359

Missiakas96a: Missiakas D, Schwager F, Betton JM, Georgopoulos C, Raina S (1996). "Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli." EMBO J 15(24);6899-909. PMID: 9003766

Nakasono00: Nakasono S, Saiki H (2000). "Effect of ELF magnetic fields on protein synthesis in Escherichia coli K12." Radiat Res 154(2);208-16. PMID: 10931694

Park08a: Park E, Lee JW, Eom SH, Seol JH, Chung CH (2008). "Binding of MG132 or deletion of the Thr active sites in HslV subunits increases the affinity of HslV protease for HslU ATPase and makes this interaction nucleotide-independent." J Biol Chem 283(48);33258-66. PMID: 18838376

Park13: Park E, Lee JW, Yoo HM, Ha BH, An JY, Jeon YJ, Seol JH, Eom SH, Chung CH (2013). "Structural alteration in the pore motif of the bacterial 20S proteasome homolog HslV leads to uncontrolled protein degradation." J Mol Biol 425(16);2940-54. PMID: 23707406

Peruski94: Peruski LF, Neidhardt FC (1994). "Identification of a conditionally essential heat shock protein in Escherichia coli." Biochim Biophys Acta 1207(2);165-72. PMID: 8075150

Rashid12: Rashid Y, Kamran Azim M, Saify ZS, Khan KM, Khan R (2012). "Small molecule activators of proteasome-related HslV peptidase." Bioorg Med Chem Lett 22(19);6089-94. PMID: 22959519

Rohrwild96: Rohrwild M, Coux O, Huang HC, Moerschell RP, Yoo SJ, Seol JH, Chung CH, Goldberg AL (1996). "HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome." Proc Natl Acad Sci U S A 93(12);5808-13. PMID: 8650174

Rohrwild97: Rohrwild M, Pfeifer G, Santarius U, Muller SA, Huang HC, Engel A, Baumeister W, Goldberg AL (1997). "The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome." Nat Struct Biol 4(2);133-9. PMID: 9033594

RuizGonzalez06: Ruiz-Gonzalez MX, Marin I (2006). "Proteasome-related HslU and HslV genes typical of eubacteria are widespread in eukaryotes." J Mol Evol 63(4);504-12. PMID: 17021930

Sauer04: Sauer RT, Bolon DN, Burton BM, Burton RE, Flynn JM, Grant RA, Hersch GL, Joshi SA, Kenniston JA, Levchenko I, Neher SB, Oakes ES, Siddiqui SM, Wah DA, Baker TA (2004). "Sculpting the proteome with AAA(+) proteases and disassembly machines." Cell 119(1);9-18. PMID: 15454077

Schmidt09a: Schmidt R, Bukau B, Mogk A (2009). "Principles of general and regulatory proteolysis by AAA+ proteases in Escherichia coli." Res Microbiol 160(9);629-36. PMID: 19781640

Seol97: Seol JH, Yoo SJ, Shin DH, Shim YK, Kang MS, Goldberg AL, Chung CH (1997). "The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase." Eur J Biochem 247(3);1143-50. PMID: 9288941

Seong02: Seong IS, Kang MS, Choi MK, Lee JW, Koh OJ, Wang J, Eom SH, Chung CH (2002). "The C-terminal tails of HslU ATPase act as a molecular switch for activation of HslV peptidase." J Biol Chem 277(29);25976-82. PMID: 12011053

Seong99: Seong IS, Oh JY, Yoo SJ, Seol JH, Chung CH (1999). "ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli." FEBS Lett 456(1);211-4. PMID: 10452560

Shi14: Shi L, Kay LE (2014). "Tracing an allosteric pathway regulating the activity of the HslV protease." Proc Natl Acad Sci U S A 111(6);2140-5. PMID: 24469799

Shin96: Shin DH, Yoo SJ, Shim YK, Seol JH, Kang MS, Chung CH (1996). "Mutational analysis of the ATP-binding site in HslU, the ATPase component of HslVU protease in Escherichia coli." FEBS Lett 398(2-3);151-4. PMID: 8977096

Slominska03: Slominska M, Wahl A, Wegrzyn G, Skarstad K (2003). "Degradation of mutant initiator protein DnaA204 by proteases ClpP, ClpQ and Lon is prevented when DNA is SeqA-free." Biochem J 370(Pt 3);867-71. PMID: 12479794

Song00: Song HK, Hartmann C, Ramachandran R, Bochtler M, Behrendt R, Moroder L, Huber R (2000). "Mutational studies on HslU and its docking mode with HslV." Proc Natl Acad Sci U S A 97(26);14103-8. PMID: 11114186

Sousa00: Sousa MC, Trame CB, Tsuruta H, Wilbanks SM, Reddy VS, McKay DB (2000). "Crystal and solution structures of an HslUV protease-chaperone complex." Cell 103(4);633-43. PMID: 11106733

Sundar10: Sundar S, McGinness KE, Baker TA, Sauer RT (2010). "Multiple sequence signals direct recognition and degradation of protein substrates by the AAA+ protease HslUV." J Mol Biol 403(3);420-9. PMID: 20837023

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Wang01: Wang J, Song JJ, Seong IS, Franklin MC, Kamtekar S, Eom SH, Chung CH (2001). "Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU." Structure (Camb) 9(11);1107-16. PMID: 11709174

Wang01a: Wang J, Song JJ, Franklin MC, Kamtekar S, Im YJ, Rho SH, Seong IS, Lee CS, Chung CH, Eom SH (2001). "Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism." Structure (Camb) 9(2);177-84. PMID: 11250202

Wang01d: Wang J (2001). "A corrected quaternary arrangement of the peptidase HslV and atpase HslU in a cocrystal structure." J Struct Biol 134(1);15-24. PMID: 11469873

Wang03a: Wang J (2003). "A second response in correcting the HslV-HslU quaternary structure." J Struct Biol 141(1);7-8. PMID: 12576015

Wang98d: Wang J, Hartling JA, Flanagan JM (1998). "Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask." J Struct Biol 124(2-3);151-63. PMID: 10049803

Wu99: Wu WF, Zhou Y, Gottesman S (1999). "Redundant in vivo proteolytic activities of Escherichia coli Lon and the ClpYQ (HslUV) protease." J Bacteriol 181(12);3681-7. PMID: 10368141

Yakamavich08: Yakamavich JA, Baker TA, Sauer RT (2008). "Asymmetric nucleotide transactions of the HslUV protease." J Mol Biol 380(5);946-57. PMID: 18582897

Yoo96: Yoo SJ, Seol JH, Shin DH, Rohrwild M, Kang MS, Tanaka K, Goldberg AL, Chung CH (1996). "Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli." J Biol Chem 271(24);14035-40. PMID: 8662828

Yoo96a: Yoo SJ, Seol JH, Kang MS, Chung CH (1996). "Poly-L-lysine activates both peptide and ATP hydrolysis by the ATP-dependent HslVU protease in Escherichia coli." Biochem Biophys Res Commun 229(2);531-5. PMID: 8954932

Yoo97: Yoo SJ, Shim YK, Seong IS, Seol JH, Kang MS, Chung CH (1997). "Mutagenesis of two N-terminal Thr and five Ser residues in HslV, the proteolytic component of the ATP-dependent HslVU protease." FEBS Lett 412(1);57-60. PMID: 9257689

Yoo97a: Yoo SJ, Seol JH, Seong IS, Kang MS, Chung CH (1997). "ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli." Biochem Biophys Res Commun 238(2);581-5. PMID: 9299555

Yoo98: Yoo SJ, Kim HH, Shin DH, Lee CS, Seong IS, Seol JH, Shimbara N, Tanaka K, Chung CH (1998). "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 273(36);22929-35. PMID: 9722513

Other References Related to Gene Regulation

Lien09a: Lien HY, Yu CH, Liou CM, Wu WF (2009). "Regulation of clpQY (hslVU) Gene Expression in Escherichia coli." Open Microbiol J 3;29-39. PMID: 19440251

Nonaka06: Nonaka G, Blankschien M, Herman C, Gross CA, Rhodius VA (2006). "Regulon and promoter analysis of the E. coli heat-shock factor, sigma32, reveals a multifaceted cellular response to heat stress." Genes Dev 20(13);1776-89. PMID: 16818608

Wade06: Wade JT, Roa DC, Grainger DC, Hurd D, Busby SJ, Struhl K, Nudler E (2006). "Extensive functional overlap between sigma factors in Escherichia coli." Nat Struct Mol Biol 13(9);806-14. PMID: 16892065

Wagner09: Wagner MA, Zahrl D, Rieser G, Koraimann G (2009). "Growth phase- and cell division-dependent activation and inactivation of the {sigma}32 regulon in Escherichia coli." J Bacteriol 191(5);1695-702. PMID: 19114495

Zahrl06: Zahrl D, Wagner M, Bischof K, Koraimann G (2006). "Expression and assembly of a functional type IV secretion system elicit extracytoplasmic and cytoplasmic stress responses in Escherichia coli." J Bacteriol 188(18);6611-21. PMID: 16952953

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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