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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2003-10-10
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pubmed:abstractText |
In the bacterial cytosol, degradation of ssrA-tagged proteins is primarily carried out by the proteolytic machine ClpXP in a process which is stimulated by a ClpX-specific adaptor protein, SspB. Here we elucidate the steps required for binding and transfer of ssrA-tagged substrates from SspB to ClpX. The N-terminal region of SspB is essential for its interaction with ssrA-tagged substrates, while a short conserved region at the C terminus of SspB interacts specifically with the N domain of ClpX. A single point mutation within the conserved C-terminal region of SspB is sufficient to abolish the SspB-mediated degradation of ssrA-tagged proteins by ClpXP. We propose that this region represents a common motif for the recognition of ClpX as the C-terminal region of SspB shares considerable homology with the other ClpX-specific adaptor protein, RssB. Through docking of SspB to the N-terminal domain of ClpX, the substrate is delivered to the substrate binding site in ClpX.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adhesins, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ClpX protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase Clp,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/salivary agglutinin receptor...,
http://linkedlifedata.com/resource/pubmed/chemical/tmRNA
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
373-80
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pubmed:dateRevised |
2009-9-3
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pubmed:meshHeading |
pubmed-meshheading:14536077-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:14536077-Adenosine Triphosphatases,
pubmed-meshheading:14536077-Adenosine Triphosphate,
pubmed-meshheading:14536077-Adhesins, Bacterial,
pubmed-meshheading:14536077-Amino Acid Motifs,
pubmed-meshheading:14536077-Amino Acid Sequence,
pubmed-meshheading:14536077-Bacterial Physiological Phenomena,
pubmed-meshheading:14536077-Bacterial Proteins,
pubmed-meshheading:14536077-Endopeptidase Clp,
pubmed-meshheading:14536077-Escherichia coli Proteins,
pubmed-meshheading:14536077-Green Fluorescent Proteins,
pubmed-meshheading:14536077-Luminescent Proteins,
pubmed-meshheading:14536077-Models, Biological,
pubmed-meshheading:14536077-Molecular Chaperones,
pubmed-meshheading:14536077-Molecular Sequence Data,
pubmed-meshheading:14536077-Multigene Family,
pubmed-meshheading:14536077-Peptides,
pubmed-meshheading:14536077-Plasmids,
pubmed-meshheading:14536077-Protein Binding,
pubmed-meshheading:14536077-Protein Structure, Secondary,
pubmed-meshheading:14536077-Protein Structure, Tertiary,
pubmed-meshheading:14536077-RNA, Bacterial,
pubmed-meshheading:14536077-Sequence Homology, Amino Acid,
pubmed-meshheading:14536077-Spectrophotometry,
pubmed-meshheading:14536077-Time Factors
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pubmed:year |
2003
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pubmed:articleTitle |
Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX.
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pubmed:affiliation |
Zentrum für Molekulare Biologie Heidelberg, Universität Heidelberg, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany. d.dougan@zmbh.uni-heidelberg.de
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pubmed:publicationType |
Journal Article
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