Linked Life Data

2153103

Source:http://linkedlifedata.com/resource/pubmed/id/2153103

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-2-21
pubmed:abstractText
In this report we have taken the reconstitution approach to study which subunits of the heterotrimer core polymerase (alpha, epsilon, theta) participate in the highly processive replication of long DNA templates by DNA polymerase III holoenzyme (holoenzyme). Comparison of the core and the alpha epsilon complex (the DNA polymerase and 3'-5' exonuclease subunits, respectively) shows they are both rapid and highly processive polymerases when they are reconstituted into a holoenzyme with the gamma complex (gamma delta delta' chi psi) and beta accessory proteins of holoenzyme. Specifically, holoenzyme reconstituted using either core or alpha epsilon completely replicates a uniquely primed 5.4-kilobase (kb) single-stranded DNA within 12 s in one binding event. Hence the theta subunit of core is not required for the processivity or speed of the holoenzyme. In contrast, when only the alpha subunit is reconstituted into the holoenzyme it is unable to replicate the entire 5.4-kb circle in one binding event but still retains a fairly high processivity of 1-3 kb and when given sufficient time for multiple binding events it finally finishes the entire circle. Therefore, highly processive DNA synthesis by holoenzyme is contingent on the epsilon exonuclease subunit. In light of these results the significance of the polymerase and exonuclease activities residing in two separate polypeptides is discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1171-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Processive replication is contingent on the exonuclease subunit of DNA polymerase III holoenzyme.
pubmed:affiliation
Microbiology Department, Hearst Microbiology Research Center, Cornell University Medical College, New York, New York 10021.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.