| pubmed-article:10486262 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10486262 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10486262 | lifeskim:mentions | umls-concept:C0015435 | lld:lifeskim |
| pubmed-article:10486262 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10486262 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10486262 | pubmed:dateCreated | 1999-10-21 | lld:pubmed |
| pubmed-article:10486262 | pubmed:abstractText | Two different yeast two hybrid systems were used to examine interaction between the partition proteins SopA and SopB of F plasmid as well as their self association. In one system, the yeast Gal4 protein DNA binding domain (Gal4-BD) is fused to the N-terminus of the bait protein, and the Gal4 activation domain (Gal4-AD) is fused to the N-terminus of the target protein (1). In the other system, the target hybrid remains unchanged but E. coli LexA protein (LexA) is fused to the C-terminus of the bait protein (2). It is found that C-terminus part of SopB is involved in interaction with itself, as an N-terminal truncation of SopB, SopB-(120-323) remains capable of self association. For interaction between SopA, deletion of the N-terminal part weakens but does not abolish the interaction. Interaction between SopB and SopA protein was also detected, but only by the use of the second system. Full length SopB [SopB-(1-323)] or SopB-(1-180) lacking the C-terminal region beyond amino acid 180 can interact with full-length SopA-(1-383) protein. | lld:pubmed |
| pubmed-article:10486262 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10486262 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10486262 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10486262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10486262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10486262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10486262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10486262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10486262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10486262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10486262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10486262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10486262 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10486262 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:10486262 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:10486262 | pubmed:author | pubmed-author:ShioHH | lld:pubmed |
| pubmed-article:10486262 | pubmed:author | pubmed-author:KimS KSK | lld:pubmed |
| pubmed-article:10486262 | pubmed:copyrightInfo | Copyright 1999 Academic Press. | lld:pubmed |
| pubmed-article:10486262 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10486262 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:10486262 | pubmed:volume | 263 | lld:pubmed |
| pubmed-article:10486262 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10486262 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10486262 | pubmed:pagination | 113-7 | lld:pubmed |
| pubmed-article:10486262 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10486262 | pubmed:meshHeading | pubmed-meshheading:10486262... | lld:pubmed |
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| pubmed-article:10486262 | pubmed:meshHeading | pubmed-meshheading:10486262... | lld:pubmed |
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| pubmed-article:10486262 | pubmed:meshHeading | pubmed-meshheading:10486262... | lld:pubmed |
| pubmed-article:10486262 | pubmed:meshHeading | pubmed-meshheading:10486262... | lld:pubmed |
| pubmed-article:10486262 | pubmed:meshHeading | pubmed-meshheading:10486262... | lld:pubmed |
| pubmed-article:10486262 | pubmed:meshHeading | pubmed-meshheading:10486262... | lld:pubmed |
| pubmed-article:10486262 | pubmed:meshHeading | pubmed-meshheading:10486262... | lld:pubmed |
| pubmed-article:10486262 | pubmed:meshHeading | pubmed-meshheading:10486262... | lld:pubmed |
| pubmed-article:10486262 | pubmed:meshHeading | pubmed-meshheading:10486262... | lld:pubmed |
| pubmed-article:10486262 | pubmed:meshHeading | pubmed-meshheading:10486262... | lld:pubmed |
| pubmed-article:10486262 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10486262 | pubmed:articleTitle | Interaction between F plasmid partition proteins SopA and SopB. | lld:pubmed |
| pubmed-article:10486262 | pubmed:affiliation | Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts 02138, USA. skkim@jcwang.harvard.edu | lld:pubmed |
| pubmed-article:10486262 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10486262 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:10486262 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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