Publication Date:
2000-09-29
Description:
Events that stall bacterial protein synthesis activate the ssrA-tagging machinery, resulting in resumption of translation and addition of an 11-residue peptide to the carboxyl terminus of the nascent chain. This ssrA-encoded peptide tag marks the incomplete protein for degradation by the energy-dependent ClpXP protease. Here, a ribosome-associated protein, SspB, was found to bind specifically to ssrA-tagged proteins and to enhance recognition of these proteins by ClpXP. Cells with an sspB mutation are defective in degrading ssrA-tagged proteins, demonstrating that SspB is a specificity-enhancing factor for ClpXP that controls substrate choice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levchenko, I -- Seidel, M -- Sauer, R T -- Baker, T A -- AI-16892/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 29;289(5488):2354-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Howard Hughes Medical Institute, Building 68, Room 523, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11009422" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Triphosphatases/*metabolism
;
Bacterial Proteins/genetics/*metabolism
;
Endopeptidase Clp
;
Escherichia coli/enzymology/*metabolism
;
*Escherichia coli Proteins
;
Green Fluorescent Proteins
;
Luminescent Proteins/metabolism
;
Mutation
;
Oligopeptides/chemistry/genetics/*metabolism
;
Operon
;
Ribosomes/metabolism
;
Serine Endopeptidases/*metabolism
;
Substrate Specificity
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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