| pubmed-article:18028309 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18028309 | lifeskim:mentions | umls-concept:C0040674 | lld:lifeskim |
| pubmed-article:18028309 | lifeskim:mentions | umls-concept:C0598312 | lld:lifeskim |
| pubmed-article:18028309 | lifeskim:mentions | umls-concept:C1429001 | lld:lifeskim |
| pubmed-article:18028309 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:18028309 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:18028309 | lifeskim:mentions | umls-concept:C0597603 | lld:lifeskim |
| pubmed-article:18028309 | lifeskim:mentions | umls-concept:C2698172 | lld:lifeskim |
| pubmed-article:18028309 | lifeskim:mentions | umls-concept:C1708533 | lld:lifeskim |
| pubmed-article:18028309 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:18028309 | pubmed:dateCreated | 2007-11-29 | lld:pubmed |
| pubmed-article:18028309 | 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. | lld:pubmed |
| pubmed-article:18028309 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18028309 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18028309 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18028309 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18028309 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18028309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18028309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18028309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18028309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18028309 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18028309 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18028309 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:18028309 | pubmed:issn | 0950-382X | lld:pubmed |
| pubmed-article:18028309 | pubmed:author | pubmed-author:NakaiHiroshiH | lld:pubmed |
| pubmed-article:18028309 | pubmed:author | pubmed-author:NorthStella... | lld:pubmed |
| pubmed-article:18028309 | pubmed:author | pubmed-author:KirtlandSandy... | lld:pubmed |
| pubmed-article:18028309 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18028309 | pubmed:volume | 66 | lld:pubmed |
| pubmed-article:18028309 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18028309 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18028309 | pubmed:pagination | 1566-78 | lld:pubmed |
| pubmed-article:18028309 | pubmed:meshHeading | pubmed-meshheading:18028309... | lld:pubmed |
| pubmed-article:18028309 | pubmed:meshHeading | pubmed-meshheading:18028309... | lld:pubmed |
| pubmed-article:18028309 | pubmed:meshHeading | pubmed-meshheading:18028309... | lld:pubmed |
| pubmed-article:18028309 | pubmed:meshHeading | pubmed-meshheading:18028309... | lld:pubmed |
| pubmed-article:18028309 | pubmed:meshHeading | pubmed-meshheading:18028309... | lld:pubmed |
| pubmed-article:18028309 | pubmed:meshHeading | pubmed-meshheading:18028309... | lld:pubmed |
| pubmed-article:18028309 | pubmed:meshHeading | pubmed-meshheading:18028309... | lld:pubmed |
| pubmed-article:18028309 | pubmed:meshHeading | pubmed-meshheading:18028309... | lld:pubmed |
| pubmed-article:18028309 | pubmed:meshHeading | pubmed-meshheading:18028309... | lld:pubmed |
| pubmed-article:18028309 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:18028309 | pubmed:articleTitle | Translation factor IF2 at the interface of transposition and replication by the PriA-PriC pathway. | lld:pubmed |
| pubmed-article:18028309 | 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. | lld:pubmed |
| pubmed-article:18028309 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18028309 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18028309 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18028309 | lld:pubmed |
