Linked Life Data

6262327

Source:http://linkedlifedata.com/resource/pubmed/id/6262327

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1981-7-20
pubmed:abstractText
The general priming system of dnaB protein and primase (Arai, K., and Kornberg, A. (1979) Proc. Natl. Acad. Sci. U. S. A. 76, 4308-4312) when compared with priming by RNA polymerase shows a number of striking differences. The general priming system is initiated primarily at single-stranded region(S), being active only on single-stranded DNAs (phages and homopolymers) and inhibited by single-stranded DNA binding protein (SSB). Transcripts are only 10 to 60 residues long. By contrast, RNA priming by RNA polymerase is initiated at base-paired regions that are not destabilized by SSB (Geider, K., Beck, E., and Schaller, H. (1978) Proc. Natl. Acad. Sci. U. S. A. 76, 645-649) and transcripts on DNA not coated with SSB are generally longer. In general priming, ATP (or GTP) has three functions: (i) an allosteric effect on dnaB protein in which the nonhydrolyzed analogs adenosine-5'-O-(3'-thiotriphosphate) (or guanosine-5'-O-(3'-thiotriphosphate) can substitute, (ii) initiation of primer synthesis which can incorporate deoxy-, as well as ribonucleotides, and (iii) elongation of the primer, in which the beta, gamma-imido analog can replace ATP (or GTP). An allosteric effect of ATP on RNA polymerase has not been demonstrated, nor has the facile synthesis of hybrid transcripts of ribo- and deoxyribonucleotides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5267-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Mechanism of dnaB protein action. IV. General priming of DNA replication by dnaB protein and primase compared with RNA polymerase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't