6pxi
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/HSLV_ECOLI HSLV_ECOLI] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.<ref>PMID:8662828</ref> <ref>PMID:8650174</ref> <ref>PMID:9288941</ref> <ref>PMID:9393683</ref> <ref>PMID:10452560</ref> <ref>PMID:10419524</ref> <ref>PMID:15696175</ref> | [https://www.uniprot.org/uniprot/HSLV_ECOLI HSLV_ECOLI] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.<ref>PMID:8662828</ref> <ref>PMID:8650174</ref> <ref>PMID:9288941</ref> <ref>PMID:9393683</ref> <ref>PMID:10452560</ref> <ref>PMID:10419524</ref> <ref>PMID:15696175</ref> | ||
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| - | == 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. | ||
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| - | 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<ref>PMID:33472065</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 6pxi" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
The crystal structure of a singly capped HslUV complex with an axial pore plug and a HslU E257Q mutation
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