clpA

Summary

Gene Symbol: clpA
Description: ATPase and specificity subunit of ClpA-ClpP ATP-dependent serine protease, chaperone activity
Alias: ECK0873, JW0866, lopD
Species: Escherichia coli str. K-12 substr. MG1655
Products:     clpA

Top Publications

  1. Houry W. Chaperone-assisted protein folding in the cell cytoplasm. Curr Protein Pept Sci. 2001;2:227-44 pubmed
    ..Several advances have recently been made in characterizing the structure and function of all of these chaperone systems. These advances have provided us with a better understanding of the protein folding process in the cell. ..
  2. Miller J, Lucius A. ATP?S competes with ATP for binding at Domain 1 but not Domain 2 during ClpA catalyzed polypeptide translocation. Biophys Chem. 2014;185:58-69 pubmed publisher
    ClpAP is an ATP-dependent protease that assembles through the association of hexameric rings of ClpA with the cylindrically-shaped protease ClpP. ClpA contains two nucleotide binding domains, termed Domain 1 (D1) or 2 (D2)...
  3. Sharma S, Hoskins J, Wickner S. Binding and degradation of heterodimeric substrates by ClpAP and ClpXP. J Biol Chem. 2005;280:5449-55 pubmed
    b>ClpA and ClpX function both as molecular chaperones and as the regulatory components of ClpAP and ClpXP proteases, respectively...
  4. Rajendar B, Lucius A. Molecular mechanism of polypeptide translocation catalyzed by the Escherichia coli ClpA protein translocase. J Mol Biol. 2010;399:665-79 pubmed publisher
    ..Here, we demonstrate that Escherichia coli ClpA, in the absence of the proteolytic component ClpP, processively and directionally steps along the polypeptide ..
  5. Seol J, Yoo S, Kim K, Kang M, Ha D, Chung C. The 65-kDa protein derived from the internal translational initiation site of the clpA gene inhibits the ATP-dependent protease Ti in Escherichia coli. J Biol Chem. 1994;269:29468-73 pubmed
    The clpA gene that encodes the ATPase subunit of the ATP-dependent protease Ti (Clp) in Escherichia coli contains a putative internal translational initiation site...
  6. Farrell C, Grossman A, Sauer R. Cytoplasmic degradation of ssrA-tagged proteins. Mol Microbiol. 2005;57:1750-61 pubmed
    ..Levels of ClpA and ClpP increased about threefold during this transition, whereas ClpX, ClpS and SspB levels remained nearly ..
  7. 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
    ..protease of Escherichia coli consists of two subunits, the ClpP subunit, which has the proteolytic active site, and ClpA, which possesses ATPase activity and activates the proteolytic activity of ClpP in vitro...
  8. Grimaud R, Kessel M, Beuron F, Steven A, Maurizi M. Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J Biol Chem. 1998;273:12476-81 pubmed
    ..Competition studies showed that ClpA may have a slightly higher affinity (approximately 2-fold) for binding to ClpP...
  9. Jennings L, Lun D, Médard M, Licht S. ClpP hydrolyzes a protein substrate processively in the absence of the ClpA ATPase: mechanistic studies of ATP-independent proteolysis. Biochemistry. 2008;47:11536-46 pubmed publisher
    ..In the case of the bacterial ATP-dependent protease ClpAP, ATP hydrolysis by the ClpA component has been proposed to be required for processive proteolysis of full-length protein substrates...

More Information

Publications76

  1. Hou J, Sauer R, Baker T. Distinct structural elements of the adaptor ClpS are required for regulating degradation by ClpAP. Nat Struct Mol Biol. 2008;15:288-94 pubmed publisher
    ..Binding of six ClpS molecules to a ClpA hexamer enhanced N-end-rule substrate degradation and inhibited ssrA-tagged protein proteolysis...
  2. Hoskins J, Pak M, Maurizi M, Wickner S. The role of the ClpA chaperone in proteolysis by ClpAP. Proc Natl Acad Sci U S A. 1998;95:12135-40 pubmed
    b>ClpA, a member of the Clp/Hsp100 family of ATPases, is a molecular chaperone and, in combination with a proteolytic component ClpP, participates in ATP-dependent proteolysis...
  3. Maurizi M, Singh S, Thompson M, Kessel M, Ginsburg A. Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP. Biochemistry. 1998;37:7778-86 pubmed
    The ClpAP protease from Escherichia coli consists of the ATP-binding regulatory component, ClpA (subunit Mr 84 165), and the proteolytic component, ClpP (subunit Mr 21 563)...
  4. Chung C, Seol J, Kang M. Protease Ti (Clp), a multi-component ATP-dependent protease in Escherichia coli. Biol Chem. 1996;377:549-54 pubmed
    The ATP-dependent protease Ti(Clp) consists of two different multimeric components: ClpA containing ATP-cleaving sites and ClpP, with serine active sites for proteolysis...
  5. Beuron F, Maurizi M, Belnap D, Kocsis E, Booy F, Kessel M, et al. At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease. J Struct Biol. 1998;123:248-59 pubmed
    ClpAP, a typical energy-dependent protease, consists of a proteolytic component (ClpP) and a chaperone-like ATPase (ClpA)...
  6. Erbse A, Schmidt R, Bornemann T, Schneider Mergener J, Mogk A, Zahn R, et al. ClpS is an essential component of the N-end rule pathway in Escherichia coli. Nature. 2006;439:753-6 pubmed
    ..In Escherichia coli, N-end rule substrates are degraded by the AAA + chaperone ClpA in complex with the ClpP peptidase (ClpAP)...
  7. Hoskins J, Wickner S. Two peptide sequences can function cooperatively to facilitate binding and unfolding by ClpA and degradation by ClpAP. Proc Natl Acad Sci U S A. 2006;103:909-14 pubmed
    ..The ClpA and ClpX ATPases of Escherichia coli generally recognize short amino acid sequences that are located near the N or ..
  8. Singh S, Guo F, Maurizi M. ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease. Biochemistry. 1999;38:14906-15 pubmed
    The Escherichia coli ClpA and ClpP proteins form a complex, ClpAP, that catalyzes ATP-dependent degradation of proteins...
  9. Maurizi M. ATP-promoted interaction between Clp A and Clp P in activation of Clp protease from Escherichia coli. Biochem Soc Trans. 1991;19:719-23 pubmed
    ..Thus the increased ATP hydrolysis is dependent on active proteolysis.(ABSTRACT TRUNCATED AT 250 WORDS) ..
  10. Wang K, Oakes E, Sauer R, Baker T. Tuning the strength of a bacterial N-end rule degradation signal. J Biol Chem. 2008;283:24600-7 pubmed publisher
    ..Together, these data define in vitro the sequence and structural requirements for the function of bacterial N-end signals. ..
  11. Katayama Y, Gottesman S, Pumphrey J, Rudikoff S, Clark W, Maurizi M. The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component. J Biol Chem. 1988;263:15226-36 pubmed
    The ATP-binding component (Component II, hereafter referred to as ClpA) of a two-component, ATP-dependent protease from Escherichia coli has been purified to homogeneity. ClpA is a protein with subunit Mr 81,000...
  12. Maglica Z, Striebel F, Weber Ban E. An intrinsic degradation tag on the ClpA C-terminus regulates the balance of ClpAP complexes with different substrate specificity. J Mol Biol. 2008;384:503-11 pubmed publisher
    ..In Escherichia coli, ClpP interacts with two alternative ATPases, ClpA or ClpX, to form active protease complexes. ClpAP and ClpXP show different but overlapping substrate specificities...
  13. Erbse A, Wagner J, Truscott K, Spall S, Kirstein J, Zeth K, et al. Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding. FEBS J. 2008;275:1400-10 pubmed publisher
    ..The ClpA component is a hexameric AAA+ (ATPase associated with various cellular activities) chaperone that utilizes the ..
  14. Kessel M, Maurizi M, Kim B, Kocsis E, Trus B, Singh S, et al. Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome. J Mol Biol. 1995;250:587-94 pubmed
    ..coli, consists of a proteolytic component, ClpP, in association with an ATP-hydrolyzing, chaperonin-like component, ClpA. To provide a structural basis for understanding the regulation and mechanism of action of Clp protease, we have ..
  15. 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. ..
  16. Singh S, Maurizi M. Mutational analysis demonstrates different functional roles for the two ATP-binding sites in ClpAP protease from Escherichia coli. J Biol Chem. 1994;269:29537-45 pubmed
    b>ClpA, the regulatory subunit of Clp protease from Escherichia coli, has two ATP-binding sites in non-homologous regions of the protein, referred to as domain I and domain II...
  17. Xia D, Esser L, Singh S, Guo F, Maurizi M. Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone. J Struct Biol. 2004;146:166-79 pubmed
    Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in the dissolution and degradation of regulatory proteins and protein aggregates...
  18. Hersch G, Burton R, Bolon D, Baker T, Sauer R. Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine. Cell. 2005;121:1017-27 pubmed
    ..These studies further emphasize commonalities between distant AAA+ family members, including protein and DNA translocases, helicases, motor proteins, clamp loaders, and other ATP-dependent enzymes. ..
  19. 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...
  20. Bohon J, Jennings L, Phillips C, Licht S, Chance M. Synchrotron protein footprinting supports substrate translocation by ClpA via ATP-induced movements of the D2 loop. Structure. 2008;16:1157-65 pubmed publisher
    Synchrotron X-ray protein footprinting is used to study structural changes upon formation of the ClpA hexamer...
  21. Gottesman S, Roche E, Zhou Y, Sauer R. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 1998;12:1338-47 pubmed
    ..with purified components and required a substrate with a wild-type SsrA tail, the presence of both ClpP and either ClpA or ClpX, and ATP...
  22. Pak M, Hoskins J, Singh S, Maurizi M, Wickner S. Concurrent chaperone and protease activities of ClpAP and the requirement for the N-terminal ClpA ATP binding site for chaperone activity. J Biol Chem. 1999;274:19316-22 pubmed
    b>ClpA, a member of the Clp/Hsp100 family of ATPases, is both an ATP-dependent molecular chaperone and the regulatory component of ClpAP protease...
  23. Seol J, Baek S, Kang M, Ha D, Chung C. Distinctive roles of the two ATP-binding sites in ClpA, the ATPase component of protease Ti in Escherichia coli. J Biol Chem. 1995;270:8087-92 pubmed
    b>ClpA is the ATPase component of the ATP-dependent protease Ti (Clp) in Escherichia coli and contains two ATP-binding sites...
  24. Rajagopal S, Sudarsan N, Nickerson K. Sodium dodecyl sulfate hypersensitivity of clpP and clpB mutants of Escherichia coli. Appl Environ Microbiol. 2002;68:4117-21 pubmed
    ..5% SDS and clpA and clpX single mutants could not grow above 5.0% SDS. For wild-type E...
  25. Ishikawa T, Maurizi M, Steven A. The N-terminal substrate-binding domain of ClpA unfoldase is highly mobile and extends axially from the distal surface of ClpAP protease. J Struct Biol. 2004;146:180-8 pubmed
    ClpAP is a barrel-like complex consisting of hexameric rings of the ClpA ATPase stacked on the double heptameric ring of ClpP peptidase. ClpA has two AAA+ domains (Dl and D2) and a 153-residue N-domain...
  26. Seol J, Kwon J, Yoo S, Kim H, Kang M, Chung C. Site-directed mutagenesis of the Cys residues in ClpA, the ATPase component of protease Ti (ClpAP) in Escherichia coli. Biol Chem. 1997;378:1205-9 pubmed
    ..been shown to be inhibited by sulfhydryl blocking agents, such as N-ethylmaleimide (NEM), when preincubated with ClpA but not with ClpP...
  27. Weber Ban E, Reid B, Miranker A, Horwich A. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature. 1999;401:90-3 pubmed
    ..b>ClpA directs the ATP-dependent degradation of substrate proteins bearing specific sequences, much as the 19S ATPase 'cap'..
  28. Singh S, Grimaud R, Hoskins J, Wickner S, Maurizi M. Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP. Proc Natl Acad Sci U S A. 2000;97:8898-903 pubmed
    ClpX and ClpA are molecular chaperones that interact with specific proteins and, together with ClpP, activate their ATP-dependent degradation...
  29. Kotova V, Manukhov I, Mel kina O, Zavil gel skiĭ G. [Mutation clpA::kan in gene encoding the chaperone of Hsp100-family decreases DnaK-dependent refolding efficiency of proteins in Escherichia coli cells]. Mol Biol (Mosk). 2008;42:1018-22 pubmed
    ..level of DnaK-dependent refolding of the thermoinactivated Vibrio fischeri luciferase were considerably lower in clpA mutant (clpA::kan) then in wild type cells...
  30. Cranz Mileva S, Imkamp F, Kolygo K, Maglica Z, Kress W, Weber Ban E. The flexible attachment of the N-domains to the ClpA ring body allows their use on demand. J Mol Biol. 2008;378:412-24 pubmed publisher
    b>ClpA is an Hsp100 chaperone that uses the chemical energy of ATP to remodel various protein substrates to prepare them for degradation...
  31. Schmidt R, Zahn R, Bukau B, Mogk A. ClpS is the recognition component for Escherichia coli substrates of the N-end rule degradation pathway. Mol Microbiol. 2009;72:506-17 pubmed publisher
    ..coli the adaptor protein ClpS directly interacts with destabilizing N-terminal residues and transfers them to the ClpA/ClpP proteolytic complex for degradation...
  32. 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. ..
  33. Choi K, Licht S. Control of peptide product sizes by the energy-dependent protease ClpAP. Biochemistry. 2005;44:13921-31 pubmed
    ..This analysis may also prove to be useful in characterizing the mechanisms of other proteases and nucleases, such as the proteasome and Dicer, which control the sizes of their products. ..
  34. Kress W, Mutschler H, Weber Ban E. Both ATPase domains of ClpA are critical for processing of stable protein structures. J Biol Chem. 2009;284:31441-52 pubmed publisher
    b>ClpA is a ring-shaped hexameric chaperone that binds to both ends of the protease ClpP and catalyzes the ATP-dependent unfolding and translocation of substrate proteins through its central pore into the ClpP cylinder...
  35. Gottesman S, Clark W, Maurizi M. The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate. J Biol Chem. 1990;265:7886-93 pubmed
    The clpA gene, which codes for the ATP-binding subunit of the ATP-dependent Clp protease of Escherichia coli, has been sequenced...
  36. Zeth K, Dougan D, Cusack S, Bukau B, Ravelli R. Crystallization and preliminary X-ray analysis of the Escherichia coli adaptor protein ClpS, free and in complex with the N-terminal domain of ClpA. Acta Crystallogr D Biol Crystallogr. 2002;58:1207-10 pubmed
    ..In most cases, these proteolytic machines are comprised of a chaperone (e.g. ClpA) that is required to prepare the substrate for degradation by the peptidase (e.g. ClpP)...
  37. Damerau K, St John A. Role of Clp protease subunits in degradation of carbon starvation proteins in Escherichia coli. J Bacteriol. 1993;175:53-63 pubmed
    ..During starvation, mutants lacking either the ClpA or ClpP subunit of the ATP-dependent Clp protease showed a partial reduction in the degradation of starvation ..
  38. Weichart D, Querfurth N, Dreger M, Hengge Aronis R. Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli. J Bacteriol. 2003;185:115-25 pubmed
    To elucidate the involvement of proteolysis in the regulation of stationary-phase adaptation, the clpA, clpX, and clpP protease mutants of Escherichia coli were subjected to proteome analysis during growth and during carbon starvation...
  39. Dougan D, Reid B, Horwich A, Bukau B. ClpS, a substrate modulator of the ClpAP machine. Mol Cell. 2002;9:673-83 pubmed
    ..Here, we report the identification of a ClpA cofactor from Escherichia coli, ClpS, which directly influences the ClpAP machine by binding to the N-terminal ..
  40. Singh S, Rozycki J, Ortega J, Ishikawa T, Lo J, Steven A, et al. Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis. J Biol Chem. 2001;276:29420-9 pubmed
    Escherichia coli ClpA and ClpX are ATP-dependent protein unfoldases that each interact with the protease, ClpP, to promote specific protein degradation...
  41. Shapiro J. A role for the Clp protease in activating Mu-mediated DNA rearrangements. J Bacteriol. 1993;175:2625-31 pubmed
    ..The clpA::Tn10 mutation, which removes a regulatory subunit of Clp protease, altered the timing of Mu activity in both ..
  42. De Donatis G, Singh S, Viswanathan S, Maurizi M. A single ClpS monomer is sufficient to direct the activity of the ClpA hexamer. J Biol Chem. 2010;285:8771-81 pubmed publisher
    ClpS is an adaptor protein that interacts with ClpA and promotes degradation of proteins with N-end rule degradation motifs (N-degrons) by ClpAP while blocking degradation of substrates with other motifs...
  43. Veronese P, Rajendar B, Lucius A. Activity of E. coli ClpA bound by nucleoside diphosphates and triphosphates. J Mol Biol. 2011;409:333-47 pubmed publisher
    The Escherichia coli ClpA protein is a molecular chaperone that binds and translocates protein substrates into the proteolytic cavity of the tetradecameric serine protease ClpP. In the absence of ClpP, ClpA can remodel protein complexes...
  44. Thomas J, Baneyx F. ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells. Mol Microbiol. 2000;36:1360-70 pubmed
    ..A number of additional proteins, including ClpA, ClpB, HtpG and IbpA/B, act as molecular chaperones in vitro, but their function in cellular protein folding ..
  45. Wang L, Elliott M, Elliott T. Conditional stability of the HemA protein (glutamyl-tRNA reductase) regulates heme biosynthesis in Salmonella typhimurium. J Bacteriol. 1999;181:1211-9 pubmed
    ..coli. Each single mutant shows only a small effect. The ClpA chaperone, but not ClpX, is required for ClpP-dependent HemA turnover...
  46. Seol J, Woo K, Kang M, Ha D, Chung C. Requirement of ATP hydrolysis for assembly of ClpA/ClpP complex, the ATP-dependent protease Ti in Escherichia coli. Biochem Biophys Res Commun. 1995;217:41-51 pubmed
    ..protease Ti (Clp) consists of two distinct components, ClpP containing the serine active sites for proteolysis and ClpA having two ATP-binding sites...
  47. 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. ..
  48. Thompson M, Maurizi M. Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates. J Biol Chem. 1994;269:18201-8 pubmed
    ..ClpAP protease is an ATP-dependent protease composed of the proteolytic component ClpP and a regulatory ATPase, ClpA. ClpAP protease degraded a variety of peptide bonds in protein and peptide substrates at a slow rate (kcat < or =..
  49. Porankiewicz J, Wang J, Clarke A. New insights into the ATP-dependent Clp protease: Escherichia coli and beyond. Mol Microbiol. 1999;32:449-58 pubmed
    ..The goal of this review is to summarize these recent findings and to highlight those areas that remain unresolved. ..
  50. 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. ..
  51. Guo F, Maurizi M, Esser L, Xia D. Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. J Biol Chem. 2002;277:46743-52 pubmed publisher
    Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in regulatory protein degradation and the dissolution and degradation of protein aggregates...
  52. Piszczek G, Rozycki J, Singh S, Ginsburg A, Maurizi M. The molecular chaperone, ClpA, has a single high affinity peptide binding site per hexamer. J Biol Chem. 2005;280:12221-30 pubmed
    ..We studied the binding of short motif-bearing peptides to ClpA, the chaperone component of the ATP-dependent ClpAP protease of Escherichia coli in the presence of ATPgammaS and ..
  53. Guo F, Esser L, Singh S, Maurizi M, Xia D. Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA. J Biol Chem. 2002;277:46753-62 pubmed
    ..coli ATP-dependent protease, ClpAP, is modulated by an adaptor protein, ClpS. ClpS binds to ClpA, the regulatory component of the ClpAP complex...
  54. Lies M, Maurizi M. Turnover of endogenous SsrA-tagged proteins mediated by ATP-dependent proteases in Escherichia coli. J Biol Chem. 2008;283:22918-29 pubmed publisher
    ..ClpAP degrades SsrA-tagged proteins slowly even in the absence of SspB, possibly because of interference from ClpA-specific substrates. Lon protease degrades SsrA-tagged proteins at a rate of approximately 0...
  55. Seol J, Yoo S, Kang M, Ha D, Chung C. The 65-kDa protein derived from the internal translational start site of the clpA gene blocks autodegradation of ClpA by the ATP-dependent protease Ti in Escherichia coli. FEBS Lett. 1995;377:41-3 pubmed
    The ATP-dependent protease Ti consists of two different components: ClpA containing ATP-cleaving sites and ClpP having serine active sites for proteolysis...
  56. Stephani K, Weichart D, Hengge R. Dynamic control of Dps protein levels by ClpXP and ClpAP proteases in Escherichia coli. Mol Microbiol. 2003;49:1605-14 pubmed
    ..This turnover is dependent on the clpP and clpX genes. The clpA gene is not required for Dps proteolysis, suggesting that Dps is a substrate for ClpXP protease but not for ClpAP ..
  57. Miller J, Lin J, Li T, Lucius A. E. coli ClpA catalyzed polypeptide translocation is allosterically controlled by the protease ClpP. J Mol Biol. 2013;425:2795-812 pubmed publisher
    ..Hexameric ClpA rings associate with one or both faces of the cylindrically shaped tetradecameric ClpP protease...
  58. Gottesman S, Squires C, Pichersky E, Carrington M, Hobbs M, Mattick J, et al. Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes. Proc Natl Acad Sci U S A. 1990;87:3513-7 pubmed
    ..tomatoes, and trypanosomes all contain genes for a large protein with extensive homology to the regulatory subunit, ClpA, of the ATP-dependent protease of Escherichia coli, Clp...
  59. 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. ..
  60. Maglica Z, Kolygo K, Weber Ban E. Optimal efficiency of ClpAP and ClpXP chaperone-proteases is achieved by architectural symmetry. Structure. 2009;17:508-16 pubmed publisher
    ..We generated asymmetric ClpP particles in which the two rings differ in ClpA and ClpX binding capability and/or in proteolytic activity...
  61. Hinnerwisch J, Fenton W, Furtak K, Farr G, Horwich A. Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell. 2005;121:1029-41 pubmed publisher
    The cylindrical Hsp100 chaperone ClpA mediates ATP-dependent unfolding of substrate proteins bearing "tag" sequences, such as the 11-residue ssrA sequence appended to proteins translationally stalled at ribosomes...
  62. Hoskins J, Yanagihara K, Mizuuchi K, Wickner S. ClpAP and ClpXP degrade proteins with tags located in the interior of the primary sequence. Proc Natl Acad Sci U S A. 2002;99:11037-42 pubmed
    ..We tested whether or not ClpA and ClpX can recognize tags when they are located in the interior of the primary sequence of the substrate...
  63. Lo J, Baker T, Sauer R. Characterization of the N-terminal repeat domain of Escherichia coli ClpA-A class I Clp/HSP100 ATPase. Protein Sci. 2001;10:551-9 pubmed
    The ClpA, ClpB, and ClpC subfamilies of the Clp/HSP100 ATPases contain a conserved N-terminal region of approximately 150 residues that consists of two approximate sequence repeats...
  64. Hoskins J, Kim S, Wickner S. Substrate recognition by the ClpA chaperone component of ClpAP protease. J Biol Chem. 2000;275:35361-7 pubmed
    b>ClpA, a member of the Clp/Hsp100 ATPase family, is a molecular chaperone and regulatory component of ClpAP protease...
  65. Katayama Y, Kasahara A, Kuraishi H, Amano F. Regulation of activity of an ATP-dependent protease, Clp, by the amount of a subunit, ClpA, in the growth of Escherichia coli cells. J Biochem. 1990;108:37-41 pubmed
    ..On the other hand, these drugs elevated both the Clp activity and the Clp A amount in exponentially growing cells, whose cellular ATP level was also reduced.(ABSTRACT TRUNCATED AT 250 WORDS) ..
  66. Veronese P, Stafford R, Lucius A. The Escherichia coli ClpA molecular chaperone self-assembles into tetramers. Biochemistry. 2009;48:9221-33 pubmed publisher
    The Escherichia coli ATP-dependent protease, ClpAP, is composed of the hexameric ATPase/protein-unfoldase, ClpA, and the tetradecameric proteolytic component, ClpP...
  67. Reid B, Fenton W, Horwich A, Weber Ban E. ClpA mediates directional translocation of substrate proteins into the ClpP protease. Proc Natl Acad Sci U S A. 2001;98:3768-72 pubmed
    ..g., ClpAP, ClpXP, and HslUV in prokaryotes, and the 26S proteasome in eukaryotes. Recent studies of the chaperone ClpA indicate that it mediates ATP-dependent unfolding of substrate proteins and directs their ATP-dependent ..