pubmed-article:14536077 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14536077 | lifeskim:mentions | umls-concept:C0162871 | lld:lifeskim |
pubmed-article:14536077 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:14536077 | lifeskim:mentions | umls-concept:C0011209 | lld:lifeskim |
pubmed-article:14536077 | lifeskim:mentions | umls-concept:C1135629 | lld:lifeskim |
pubmed-article:14536077 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
pubmed-article:14536077 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
pubmed-article:14536077 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
pubmed-article:14536077 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:14536077 | pubmed:dateCreated | 2003-10-10 | lld:pubmed |
pubmed-article:14536077 | 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. | lld:pubmed |
pubmed-article:14536077 | pubmed:language | eng | lld:pubmed |
pubmed-article:14536077 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14536077 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14536077 | pubmed:month | Aug | lld:pubmed |
pubmed-article:14536077 | pubmed:issn | 1097-2765 | lld:pubmed |
pubmed-article:14536077 | pubmed:author | pubmed-author:DouganDavid... | lld:pubmed |
pubmed-article:14536077 | pubmed:author | pubmed-author:BukauBerndB | lld:pubmed |
pubmed-article:14536077 | pubmed:author | pubmed-author:Weber-BanEili... | lld:pubmed |
pubmed-article:14536077 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14536077 | pubmed:volume | 12 | lld:pubmed |
pubmed-article:14536077 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14536077 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14536077 | pubmed:pagination | 373-80 | lld:pubmed |
pubmed-article:14536077 | pubmed:dateRevised | 2009-9-3 | lld:pubmed |
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pubmed-article:14536077 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:14536077 | pubmed:articleTitle | Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX. | lld:pubmed |
pubmed-article:14536077 | pubmed:affiliation | Zentrum für Molekulare Biologie Heidelberg, Universität Heidelberg, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany. d.dougan@zmbh.uni-heidelberg.de | lld:pubmed |
pubmed-article:14536077 | pubmed:publicationType | Journal Article | lld:pubmed |
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