Genomes and Genes
Gene Symbol: ECs4859
Description: ATP-dependent protease peptidase subunit
Species: Escherichia coli O157:H7 str. Sakai
- 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..A tripeptide aldehyde inhibitor, acetyl-Leu-Leu-norleucinal, binds to the N-terminal threonine residue of HslV, probably as a hemiacetal, relating HslV also functionally to the proteasomes of archaea and eukaryotes...
- 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..To our knowledge this is the first report of a eubacterial HslVU complex in eukaryotes and, consequently, of the simultaneous occurrence of both a proteasome and HslVU in living cells...
- 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..coli homologs suggest that the encoded HslV and HslU proteins function as forming an ATP-dependent protease complex as in E. coli. ..
- 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..Once these errors are corrected, a quaternary arrangement that is similar to those observed in the other structures emerges. ..
- 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..Biochemical evidence suggests that HslV/ClpQ is an efficient peptidase whose activity is enhanced by HslU/CIpY in the presence of ATP. ..
- Slominska M, Wahl A, Wegrzyn G, Skarstad K. Degradation of mutant initiator protein DnaA204 by proteases ClpP, ClpQ and Lon is prevented when DNA is SeqA-free. Biochem J. 2003;370:867-71 pubmed..Its cognate protease ClpQ, as well as Lon protease, degraded DnaA204 to the same degree as ClpP. The chaperones GroES, GroEL and DnaK contributed to stabilization of DnaA204 protein. ..
- 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..Thus, the functional requirements for ATP-dependent hydrolysis of peptides and proteins appear different. ..
- 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..These results suggest that, in the reconstituted HslVU complex, the peptide hydrolysis by HslV occurs in a tightly coupled process with the cleavage of ATP by HslU. ..
- 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..In this mechanism, unfolded polypeptides are threaded through the aligned pores of the ATPase and peptidase and translocated into the peptidase central chamber...
- 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..Moreover, similarity in their overall architecture suggests a common model for their action. ..
- 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..These results suggest that the Cys residues play an important role in maintaining the structure and function of the HslVU protease. ..
- 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..Both HslU and the P. haemolytica protein share a ATP/GTP-binding motif near their N-termini. The two operons described here are transcribed counterclockwise on the standard genetic map...
- 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..These results suggest that the mutation in the ATP-binding site results in prevention of the binding of the adenine nucleotides to HslU and hence in impairment of both oligomerization and ATPase function of HslU. ..
- 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..Therefore ATP appears necessary for oligomerization of HslU. Thus the HslVU protease appears to be a two-component protease in which HslV harbors the peptidase activity, while HslU provides an essential ATPase activity...
- Nakasono S, Saiki H. Effect of ELF magnetic fields on protein synthesis in Escherichia coli K12. Radiat Res. 2000;154:208-16 pubmed..These results suggest that 2D PAGE is sufficient to detect cell responses to environmental stress. The high-intensity ELF MFs (14 mT at power frequency) did not act as a general stress factor. ..
- 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
- 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..The symmetry mismatch previously observed between hexameric ClpA and heptameric ClpP in the related ClpAP protease is apparently not reproduced in the symmetry-matched ClpYQ system. ..
- 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 observed nucleotide-dependent conformational changes in HslU and their governing principles provide a framework for the mechanistic understanding of other AAA(+) proteins...
- 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..These results suggest that the HslU C-terminal tails act as a molecular switch for the assembly of HslVU complex and the activation of HslV peptidase...
- 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..The mutational studies also revealed that both Thr, Ser103, and Ser172, but not Ser124, are involved in the interaction of HslV with HslU and hence in the activation of HslU ATPase as well as in the HslVU complex formation. ..
- 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..These results indicate that CodWX in B.subtilis represents the first N-terminal serine protease among all known proteolytic enzymes. ..
- 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..Thus, it appears that ATP-binding, but not its hydrolysis, is essential for assembly and proteolytic activity of HslVU. ..
- 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..The structure-based multiple proteasomal alignment of 433 sequences from 143 organisms can be downloaded from the URL dagger and will be updated regularly...
- 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. ..
- Wu W, Zhou Y, Gottesman S. Redundant in vivo proteolytic activities of Escherichia coli Lon and the ClpYQ (HslUV) protease. J Bacteriol. 1999;181:3681-7 pubmed..Thus, a protease with a structure and an active site different from those of Lon is capable of recognizing and degrading two different Lon substrates and appears to act as a backup for Lon under certain conditions. ..