Journal article
An Alternative Form of Replication Protein A Prevents Viral Replication in Vitro
The Journal of biological chemistry, Vol.284(8), pp.5324-5331
02/20/2009
DOI: 10.1074/jbc.M808963200
PMCID: PMC2643524
PMID: 19116208
Abstract
Replication protein A (RPA), the eukaryotic single-stranded DNA-binding
complex, is essential for multiple processes in cellular DNA metabolism. The
“canonical” RPA is composed of three subunits (RPA1, RPA2, and
RPA3); however, there is a human homolog to the RPA2 subunit, called RPA4,
that can substitute for RPA2 in complex formation. We demonstrate that the
resulting “alternative” RPA (aRPA) complex has solution and DNA
binding properties indistinguishable from the canonical RPA complex; however,
aRPA is unable to support DNA replication and inhibits canonical RPA function.
Two regions of RPA4, the putative L34 loop and the C terminus, are responsible
for inhibiting SV40 DNA replication. Given that aRPA inhibits canonical RPA
function
in vitro
and is found in nonproliferative tissues, these
studies indicate that RPA4 expression may prevent cellular proliferation via
replication inhibition while playing a role in maintaining the viability of
quiescent cells.
Details
- Title: Subtitle
- An Alternative Form of Replication Protein A Prevents Viral Replication in Vitro
- Creators
- Aaron C Mason - Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, Iowa 52242Stuart J Haring - Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, Iowa 52242John M Pryor - Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, Iowa 52242Cathy A Staloch - Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, Iowa 52242Tze Fei Gan - Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, Iowa 52242Marc S Wold - Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, Iowa 52242
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.284(8), pp.5324-5331
- DOI
- 10.1074/jbc.M808963200
- PMID
- 19116208
- PMCID
- PMC2643524
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- American Society for Biochemistry and Molecular Biology
- Language
- English
- Date published
- 02/20/2009
- Academic Unit
- Radiation Oncology; Biochemistry and Molecular Biology
- Record Identifier
- 9984024557702771
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