| Structural highlights
Function
HSLU_ECOLI ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.[1] [2] [3] [4] [5] [6] [7]
Publication Abstract from PubMed
At low temperatures, protein degradation by the AAA+ HslUV protease is very slow. New crystal structures reveal that residues in the intermediate domain of the HslU(6) unfoldase can plug its axial channel, blocking productive substrate binding and subsequent unfolding, translocation, and degradation by the HslV(12) peptidase. Biochemical experiments with wild-type and mutant enzymes support a model in which heat-induced melting of this autoinhibitory plug activates HslUV proteolysis.
Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug.,Baytshtok V, Fei X, Shih TT, Grant RA, Santos JC, Baker TA, Sauer RT Cell Rep. 2021 Jan 19;34(3):108639. doi: 10.1016/j.celrep.2020.108639. PMID:33472065[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yoo SJ, Seol JH, Shin DH, Rohrwild M, Kang MS, Tanaka K, Goldberg AL, Chung CH. 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 Jun 14;271(24):14035-40. PMID:8662828
- ↑ Rohrwild M, Coux O, Huang HC, Moerschell RP, Yoo SJ, Seol JH, Chung CH, Goldberg 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 Jun 11;93(12):5808-13. PMID:8650174
- ↑ Seol JH, Yoo SJ, Shin DH, Shim YK, Kang MS, Goldberg AL, Chung CH. The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase. Eur J Biochem. 1997 Aug 1;247(3):1143-50. PMID:9288941
- ↑ Kanemori M, Nishihara K, Yanagi H, Yura T. Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli. J Bacteriol. 1997 Dec;179(23):7219-25. PMID:9393683
- ↑ Seong IS, Oh JY, Yoo SJ, Seol JH, Chung CH. ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli. FEBS Lett. 1999 Jul 30;456(1):211-4. PMID:10452560
- ↑ 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 Jul 30;274(31):22002-7. PMID:10419524
- ↑ Burton RE, Baker TA, Sauer RT. Nucleotide-dependent substrate recognition by the AAA+ HslUV protease. Nat Struct Mol Biol. 2005 Mar;12(3):245-51. Epub 2005 Feb 6. PMID:15696175 doi:10.1038/nsmb898
- ↑ Baytshtok V, Fei X, Shih TT, Grant RA, Santos JC, Baker TA, Sauer RT. Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug. Cell Rep. 2021 Jan 19;34(3):108639. PMID:33472065 doi:10.1016/j.celrep.2020.108639
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