Category:Complex:ClpAP
About
Description (originally from EcoCyc[1]) ClpAP
Comments (originally from EcoCyc[1]) ClpAP is a serine protease complex responsible for the ATP-dependent degradation of a number of proteins [2][3][4][5][6][7][8][9][10][11][12][13][14][12][15][16][17][18][19][20][21].
References
- ↑ 1.0 1.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ Katayama, Y et al. (1988) The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component. J. Biol. Chem. 263 15226-36 PubMed
- ↑ Wickner, S et al. (1994) A molecular chaperone, ClpA, functions like DnaK and DnaJ. Proc. Natl. Acad. Sci. U.S.A. 91 12218-22 PubMed
- ↑ Wang, L et al. (1999) Conditional stability of the HemA protein (glutamyl-tRNA reductase) regulates heme biosynthesis in Salmonella typhimurium. J. Bacteriol. 181 1211-9 PubMed
- ↑ Damerau, K & St John, AC (1993) Role of Clp protease subunits in degradation of carbon starvation proteins in Escherichia coli. J. Bacteriol. 175 53-63 PubMed
- ↑ Gottesman, S et al. (1998) The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12 1338-47 PubMed
- ↑ Weber-Ban, EU et al. (1999) Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature 401 90-3 PubMed
- ↑ Gottesman, S et al. (1993) ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities. J. Biol. Chem. 268 22618-26 PubMed
- ↑ Tobias, JW et al. (1991) The N-end rule in bacteria. Science 254 1374-7 PubMed
- ↑ Kessel, M et al. (1995) Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome. J. Mol. Biol. 250 587-94 PubMed
- ↑ Ishikawa, T et al. () 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. 146 180-8 PubMed
- ↑ 12.0 12.1 Thompson, MW et al. (1994) Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis. J. Biol. Chem. 269 18209-15 PubMed
- ↑ Seol, JH et al. (1995) Requirement of ATP hydrolysis for assembly of ClpA/ClpP complex, the ATP-dependent protease Ti in Escherichia coli. Biochem. Biophys. Res. Commun. 217 41-51 PubMed
- ↑ Maurizi, MR et al. (1998) Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP. Biochemistry 37 7778-86 PubMed
- ↑ Singh, SK et al. (1999) ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease. Biochemistry 38 14906-15 PubMed
- ↑ Thompson, MW & Maurizi, MR (1994) Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates. J. Biol. Chem. 269 18201-8 PubMed
- ↑ Seol, JH et al. (1994) 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. 269 29468-73 PubMed
- ↑ Dougan, DA et al. (2002) ClpS, a substrate modulator of the ClpAP machine. Mol. Cell 9 673-83 PubMed
- ↑ Zeth, K et al. (2002) Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. Nat. Struct. Biol. 9 906-11 PubMed
- ↑ Katayama, Y et al. (1990) 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. 108 37-41 PubMed
- ↑ Stephani, K et al. (2003) Dynamic control of Dps protein levels by ClpXP and ClpAP proteases in Escherichia coli. Mol. Microbiol. 49 1605-14 PubMed
This category currently contains no pages or media.
