| pubmed-article:12949107 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12949107 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:12949107 | lifeskim:mentions | umls-concept:C0036111 | lld:lifeskim |
| pubmed-article:12949107 | lifeskim:mentions | umls-concept:C1947951 | lld:lifeskim |
| pubmed-article:12949107 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:12949107 | lifeskim:mentions | umls-concept:C0243111 | lld:lifeskim |
| pubmed-article:12949107 | lifeskim:mentions | umls-concept:C0699789 | lld:lifeskim |
| pubmed-article:12949107 | lifeskim:mentions | umls-concept:C0440043 | lld:lifeskim |
| pubmed-article:12949107 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:12949107 | pubmed:dateCreated | 2003-9-1 | lld:pubmed |
| pubmed-article:12949107 | pubmed:abstractText | FliJ, a 17-kDa protein, is a soluble component of the Salmonella type III flagellar protein export system that has antiaggregation properties and several other characteristics that suggest it may have a chaperone-like function. We have now examined this protein in detail. Ten-amino-acid scanning deletions covering the entire 147-amino-acid sequence were tested for complementation of a fliJ null strain; only the first and last deletions complemented. A few of the deletions, especially towards the C terminus, exerted a dominant negative effect on wild-type cells, indicating that they were actively interfering with function. Two truncated versions of FliJ, representing its N- and C-terminal halves, failed to complement and were not dominant. We tested for FliJ self-association by several techniques. Size-exclusion chromatography (Superdex 200) indicated an apparent molecular mass of around 50 kDa, which could reflect either multimerization or an elongated shape or both. Multiangle light scattering gave a peak value of 20 kDa, close to the molecular mass of the monomer. Analytical ultracentrifugation gave evidence for weak self-association as a trimer or tetramer. It was known from previous studies that FliJ interacts with the N-terminal region of FliH, a negative regulator of the ATPase FliI. Using both truncation and deletion versions of FliJ, we now show that it is its C-terminal region that is responsible for this interaction. We also show that FliJ interacts with the soluble cytoplasmic domain of the largest membrane component of the export apparatus, FlhA; although small deletions in FliJ did not interfere with the association, both truncated versions failed to associate, indicating that a substantial amount of the central region of the FliJ sequence participates in the association. We present a model summarizing these multiple interactions. | lld:pubmed |
| pubmed-article:12949107 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12949107 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12949107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12949107 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12949107 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:12949107 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:12949107 | pubmed:author | pubmed-author:MacnabRobert... | lld:pubmed |
| pubmed-article:12949107 | pubmed:author | pubmed-author:TameJeremy... | lld:pubmed |
| pubmed-article:12949107 | pubmed:author | pubmed-author:FraserGillian... | lld:pubmed |
| pubmed-article:12949107 | pubmed:author | pubmed-author:González-Pedr... | lld:pubmed |
| pubmed-article:12949107 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12949107 | pubmed:volume | 185 | lld:pubmed |
| pubmed-article:12949107 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12949107 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12949107 | pubmed:pagination | 5546-54 | lld:pubmed |
| pubmed-article:12949107 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:12949107 | pubmed:meshHeading | pubmed-meshheading:12949107... | lld:pubmed |
| pubmed-article:12949107 | pubmed:meshHeading | pubmed-meshheading:12949107... | lld:pubmed |
| pubmed-article:12949107 | pubmed:meshHeading | pubmed-meshheading:12949107... | lld:pubmed |
| pubmed-article:12949107 | pubmed:meshHeading | pubmed-meshheading:12949107... | lld:pubmed |
| pubmed-article:12949107 | pubmed:meshHeading | pubmed-meshheading:12949107... | lld:pubmed |
| pubmed-article:12949107 | pubmed:meshHeading | pubmed-meshheading:12949107... | lld:pubmed |
| pubmed-article:12949107 | pubmed:meshHeading | pubmed-meshheading:12949107... | lld:pubmed |
| pubmed-article:12949107 | pubmed:meshHeading | pubmed-meshheading:12949107... | lld:pubmed |
| pubmed-article:12949107 | pubmed:meshHeading | pubmed-meshheading:12949107... | lld:pubmed |
| pubmed-article:12949107 | pubmed:meshHeading | pubmed-meshheading:12949107... | lld:pubmed |
| pubmed-article:12949107 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12949107 | pubmed:articleTitle | Interactions of FliJ with the Salmonella type III flagellar export apparatus. | lld:pubmed |
| pubmed-article:12949107 | pubmed:affiliation | Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, USA. | lld:pubmed |
| pubmed-article:12949107 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12949107 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12949107 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:946390 | entrezgene:pubmed | pubmed-article:12949107 | lld:entrezgene |
| entrez-gene:946391 | entrezgene:pubmed | pubmed-article:12949107 | lld:entrezgene |
| entrez-gene:946456 | entrezgene:pubmed | pubmed-article:12949107 | lld:entrezgene |
| entrez-gene:946457 | entrezgene:pubmed | pubmed-article:12949107 | lld:entrezgene |
| entrez-gene:946454 | entrezgene:pubmed | pubmed-article:12949107 | lld:entrezgene |
| entrez-gene:946458 | entrezgene:pubmed | pubmed-article:12949107 | lld:entrezgene |
| entrez-gene:946462 | entrezgene:pubmed | pubmed-article:12949107 | lld:entrezgene |
| entrez-gene:946463 | entrezgene:pubmed | pubmed-article:12949107 | lld:entrezgene |
| entrez-gene:946464 | entrezgene:pubmed | pubmed-article:12949107 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12949107 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12949107 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12949107 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12949107 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12949107 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12949107 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12949107 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12949107 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12949107 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12949107 | lld:pubmed |
