Brown, G. W., Melendy, T. E., Ray, D. S. (November 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)
Preview |
PDF (Paper)
Melendy PNAS 1992.pdf - Published Version Download (1MB) | Preview |
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: | 1 November 1992 |
| Date Deposited: | 22 Sep 2015 15:11 |
| Last Modified: | 09 Nov 2017 20:12 |
| PMCID: | PMC50311 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/31852 |
Actions (login required)
 |
Administrator's edit/view item |
