Conservation of structure and function of DNA replication protein A in the trypanosomatid Crithidia fasciculata.
AUTOR(ES)
Brown, G W
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=50311Documentos Relacionados
- Pathway of protein glycosylation in the trypanosomatid Crithidia fasciculata.
- A DNase from the trypanosomatid Crithidia fasciculata.
- Introduction of plasmid DNA into the trypanosomatid protozoan Crithidia fasciculata.
- Purification and characterization of DNA ligase I from the trypanosomatid Crithidia fasciculata.
- Reverse transcriptase encoded by a retrotransposon from the trypanosomatid Crithidia fasciculata.