| pubmed-article:14976191 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14976191 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:14976191 | lifeskim:mentions | umls-concept:C0004595 | lld:lifeskim |
| pubmed-article:14976191 | lifeskim:mentions | umls-concept:C0036536 | lld:lifeskim |
| pubmed-article:14976191 | lifeskim:mentions | umls-concept:C0036537 | lld:lifeskim |
| pubmed-article:14976191 | lifeskim:mentions | umls-concept:C0162847 | lld:lifeskim |
| pubmed-article:14976191 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:14976191 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:14976191 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:14976191 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:14976191 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:14976191 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:14976191 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:14976191 | pubmed:dateCreated | 2004-4-26 | lld:pubmed |
| pubmed-article:14976191 | pubmed:abstractText | The PrsA protein of Bacillus subtilis is an essential membrane-bound lipoprotein that is assumed to assist post-translocational folding of exported proteins and stabilize them in the compartment between the cytoplasmic membrane and cell wall. This folding activity is consistent with the homology of a segment of PrsA with parvulin-type peptidyl-prolyl cis/trans isomerases (PPIase). In this study, molecular modeling showed that the parvulin-like region can adopt a parvulin-type fold with structurally conserved active site residues. PrsA exhibits PPIase activity in a manner dependent on the parvulin-like domain. We constructed deletion, peptide insertion, and amino acid substitution mutations and demonstrated that the parvulin-like domain as well as flanking N- and C-terminal domains are essential for in vivo PrsA function in protein secretion and growth. Surprisingly, none of the predicted active site residues of the parvulin-like domain was essential for growth and protein secretion, although several active site mutations reduced or abolished the PPIase activity or the ability of PrsA to catalyze proline-limited protein folding in vitro. Our results indicate that PrsA is a PPIase, but the essential role in vivo seems to depend on some non-PPIase activity of both the parvulin-like and flanking domains. | lld:pubmed |
| pubmed-article:14976191 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14976191 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976191 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14976191 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976191 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14976191 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976191 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14976191 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:14976191 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:14976191 | pubmed:author | pubmed-author:SavilahtiHarr... | lld:pubmed |
| pubmed-article:14976191 | pubmed:author | pubmed-author:HeckerMichael... | lld:pubmed |
| pubmed-article:14976191 | pubmed:author | pubmed-author:VihinenMaunoM | lld:pubmed |
| pubmed-article:14976191 | pubmed:author | pubmed-author:SarvasMattiM | lld:pubmed |
| pubmed-article:14976191 | pubmed:author | pubmed-author:KontinenVesa... | lld:pubmed |
| pubmed-article:14976191 | pubmed:author | pubmed-author:TairaSuviS | lld:pubmed |
| pubmed-article:14976191 | pubmed:author | pubmed-author:AntelmannHaik... | lld:pubmed |
| pubmed-article:14976191 | pubmed:author | pubmed-author:LappalainenIl... | lld:pubmed |
| pubmed-article:14976191 | pubmed:author | pubmed-author:BoerHarryH | lld:pubmed |
| pubmed-article:14976191 | pubmed:author | pubmed-author:VitikainenMar... | lld:pubmed |
| pubmed-article:14976191 | pubmed:author | pubmed-author:SeppalaRailiR | lld:pubmed |
| pubmed-article:14976191 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14976191 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:14976191 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:14976191 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14976191 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14976191 | pubmed:pagination | 19302-14 | lld:pubmed |
| pubmed-article:14976191 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:14976191 | pubmed:meshHeading | pubmed-meshheading:14976191... | lld:pubmed |
| pubmed-article:14976191 | pubmed:meshHeading | pubmed-meshheading:14976191... | lld:pubmed |
| pubmed-article:14976191 | pubmed:meshHeading | pubmed-meshheading:14976191... | lld:pubmed |
| pubmed-article:14976191 | pubmed:meshHeading | pubmed-meshheading:14976191... | lld:pubmed |
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| pubmed-article:14976191 | pubmed:meshHeading | pubmed-meshheading:14976191... | lld:pubmed |
| pubmed-article:14976191 | pubmed:meshHeading | pubmed-meshheading:14976191... | lld:pubmed |
| pubmed-article:14976191 | pubmed:meshHeading | pubmed-meshheading:14976191... | lld:pubmed |
| pubmed-article:14976191 | pubmed:meshHeading | pubmed-meshheading:14976191... | lld:pubmed |
| pubmed-article:14976191 | pubmed:meshHeading | pubmed-meshheading:14976191... | lld:pubmed |
| pubmed-article:14976191 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14976191 | pubmed:articleTitle | Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis. | lld:pubmed |
| pubmed-article:14976191 | pubmed:affiliation | Vaccine Development Laboratory, National Public Health Institute, Mannerheimintie 166, FIN-00300 Helsinki, Finland. | lld:pubmed |
| pubmed-article:14976191 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14976191 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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