Linked Life Data

18028309

Source:http://linkedlifedata.com/resource/pubmed/id/18028309

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2007-11-29
pubmed:abstractText
Bacteriophage Mu DNA synthesis is initiated during transposition by replication restart proteins PriA, DnaT and either PriB or PriC. The PriA-PriC pathway requires PriA's helicase activity and other host factors that promote the orderly transition from transpososome to replisome on the Mu DNA template. The host factor MRFalpha-PR, which removes obstacles to PriA binding and promotes the PriA-PriC pathway, was identified to be the translation initiation factor IF2. Purified isoform IF2-2, which is truncated at the N-terminal end, had full MRFalpha-PR activity whereas full-length IF2-1 was inactive. IF2-2 was bound to the Mu DNA template specifically at the step for prereplisome assembly. Prior steps in the orderly transition from transpososome were essential to promote efficient IF2-2 binding. Moreover, PriA helicase activity was subsequently needed to displace IF2-2, remodelling the template to permit replisome assembly. IF2's role in the transition mechanism as well as its function as G protein and translation factor suggest its potential to regulate DNA synthesis by this pathway.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1566-78
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Translation factor IF2 at the interface of transposition and replication by the PriA-PriC pathway.
pubmed:affiliation
Department of Biochemistry and Molecular & Cellular Biology, Georgetown University Medical Center, Rm. 331 Basic Science Bldg., 3900 Reservoir Road NW, Washington, DC 20057-1455, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural