Conservation of structure and function of DNA replication protein A in the trypanosomatid Crithidia fasciculata

Brown, G. W., Melendy, T. E., Ray, D. S. (1992) Conservation of structure and function of DNA replication protein A in the trypanosomatid Crithidia fasciculata. Proc Natl Acad Sci U S A, 89 (21). pp. 10227-31. ISSN 0027-8424 (Print)0027-8424 (Linking)

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URL: http://www.ncbi.nlm.nih.gov/pubmed/1332038

Abstract

Human replication protein A (RP-A) is a three-subunit protein that is required for simian virus 40 (SV40) replication in vitro. The trypanosome homologue of RP-A has been purified from Crithidia fasciculata. It is a 1:1:1 complex of three polypeptides of 51, 28, and 14 kDa, binds single-stranded DNA via the large subunit, and is localized within the nucleus. C. fasciculata RP-A substitutes for human RP-A in the large tumor antigen-dependent unwinding of the SV40 origin of replication and stimulates both DNA synthesis and DNA priming by human DNA polymerase alpha/primase, but it does not support efficient SV40 DNA replication in vitro. This extraordinary conservation of structure and function between human and trypanosome RP-A suggests that the mechanism of DNA replication, at both the initiation and the elongation level, is conserved in organisms that diverged from the main eukaryotic lineage very early in evolution.

Item Type: Paper
Uncontrolled Keywords: Animals Chromatography, Affinity Crithidia fasciculata/*genetics/metabolism DNA Polymerase II/metabolism *DNA Replication DNA-Binding Proteins/isolation & purification/*metabolism DNA-Directed DNA Polymerase/metabolism Humans Macromolecular Substances Replication Protein A Simian virus 40/genetics Templates, Genetic
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > DNA polymerase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > DNA replication
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
evolution
CSHL Authors:
Communities: CSHL labs > Stillman lab
Depositing User: Matt Covey
Date Deposited: 22 Sep 2015 15:11
Last Modified: 09 Nov 2017 20:12
PMCID: PMC50311
Related URLs:
URI: http://repository.cshl.edu/id/eprint/31852

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