Linked Life Data

14530260

Source:http://linkedlifedata.com/resource/pubmed/id/14530260

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
50
pubmed:dateCreated
2003-12-8
pubmed:abstractText
Replication factor C (RFC) is a heteropentameric AAA+ protein clamp loader of the proliferating cell nuclear antigen (PCNA) processivity factor. The prokaryotic homologue, gamma complex, is also a heteropentamer, and structural studies show the subunits are arranged in a circle. In this report, Saccharomyces cerevisiae RFC protomers are examined for their interaction with each other and PCNA. The data lead to a model of subunit order around the circle. A characteristic of AAA+ oligomers is the use of bipartite ATP sites in which one subunit supplies a catalytic arginine residue for hydrolysis of ATP bound to the neighboring subunit. We find that the RFC(3/4) complex is a DNA-dependent ATPase, and we use this activity to determine that RFC3 supplies a catalytic arginine to the ATP site of RFC4. This information, combined with the subunit arrangement, defines the composition of the remaining ATP sites. Furthermore, the RFC(2/3) and RFC(3/4) subassemblies bind stably to PCNA, yet neither RFC2 nor RFC4 bind tightly to PCNA, indicating that RFC3 forms a strong contact point to PCNA. The RFC1 subunit also binds PCNA tightly, and we identify two hydrophobic residues in RFC1 that are important for this interaction. Therefore, at least two subunits in RFC make strong contacts with PCNA, unlike the Escherichia coli gamma complex in which only one subunit makes strong contact with the beta clamp. Multiple strong contact points to PCNA may reflect the extra demands of loading the PCNA trimeric ring onto DNA compared with the dimeric beta ring.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
50744-53
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:14530260-Adenosine Triphosphatases, pubmed-meshheading:14530260-Adenosine Triphosphate, pubmed-meshheading:14530260-Arginine, pubmed-meshheading:14530260-Cell Division, pubmed-meshheading:14530260-Chromatography, Gel, pubmed-meshheading:14530260-Crystallography, X-Ray, pubmed-meshheading:14530260-DNA-Binding Proteins, pubmed-meshheading:14530260-Dose-Response Relationship, Drug, pubmed-meshheading:14530260-Escherichia coli, pubmed-meshheading:14530260-Hydrolysis, pubmed-meshheading:14530260-Models, Molecular, pubmed-meshheading:14530260-Plasmids, pubmed-meshheading:14530260-Proliferating Cell Nuclear Antigen, pubmed-meshheading:14530260-Protein Binding, pubmed-meshheading:14530260-Protein Conformation, pubmed-meshheading:14530260-Protein Structure, Tertiary, pubmed-meshheading:14530260-Replication Protein C, pubmed-meshheading:14530260-Saccharomyces cerevisiae, pubmed-meshheading:14530260-Time Factors
pubmed:year
2003
pubmed:articleTitle
Replication factor C clamp loader subunit arrangement within the circular pentamer and its attachment points to proliferating cell nuclear antigen.
pubmed:affiliation
The Rockefeller University, New York, New York 1002, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't