Linked Life Data

10486262

Source:http://linkedlifedata.com/resource/pubmed/id/10486262

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-10-21
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
113-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Interaction between F plasmid partition proteins SopA and SopB.
pubmed:affiliation
Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts 02138, USA. skkim@jcwang.harvard.edu
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't