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Journal ArticleDOI

REPLICATION PROTEIN A: A Heterotrimeric, Single-Stranded DNA-Binding Protein Required for Eukaryotic DNA Metabolism

Marc S. Wold
- 01 Jan 1997 - 
- Vol. 66, Iss: 1, pp 61-92
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TLDR
Replication protein A (RPA) is a single-stranded DNA-binding protein that is required for multiple processes in eukaryotic DNA metabolism, including DNA replication, DNA repair, and recombination.
Abstract
Replication protein A [RPA; also known as replication factor A (RFA) and human single-stranded DNA-binding protein] is a single-stranded DNA-binding protein that is required for multiple processes in eukaryotic DNA metabolism, including DNA replication, DNA repair, and recombination. RPA homologues have been identified in all eukaryotic organisms examined and are all abundant heterotrimeric proteins composed of subunits of approximately 70, 30, and 14 kDa. Members of this family bind nonspecifically to single-stranded DNA and interact with and/or modify the activities of multiple proteins. In cells, RPA is phosphorylated by DNA-dependent protein kinase when RPA is bound to single-stranded DNA (during S phase and after DNA damage). Phosphorylation of RPA may play a role in coordinating DNA metabolism in the cell. RPA may also have a role in modulating gene expression.

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Citations
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Journal ArticleDOI

The DNA Damage Response: Making It Safe to Play with Knives

TL;DR: This review will focus on how the DDR controls DNA repair and the phenotypic consequences of defects in these critical regulatory functions in mammals.
Journal ArticleDOI

Sensing DNA Damage Through ATRIP Recognition of RPA-ssDNA Complexes

TL;DR: The data suggest that RPA-coated ssDNA is the critical structure at sites of DNA damage that recruits the ATR-ATRIP complex and facilitates its recognition of substrates for phosphorylation and the initiation of checkpoint signaling.
Journal ArticleDOI

Molecular mechanism of nucleotide excision repair

TL;DR: The identification of two complementation groups (CS-A and CS-B) shows that at least two gene products are specifically needed for fast and efficient repair of transcribed strands, and suggests that transcription-coupled repair and/or the CS proteins have functions beyond NER.
Journal ArticleDOI

Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications

TL;DR: How the development of various complementary methodologies has provided valuable insights into the spatiotemporal dynamics of DDR protein assembly/disassembly at sites of DNA strand breaks in eukaryotic cells is outlined.
Journal ArticleDOI

Homologous recombination in DNA repair and DNA damage tolerance

TL;DR: Mechanistic aspects of HR relating to DSB and ICL repair as well as replication fork support related to DNA double-stranded breaks and interstrand crosslinks are reviewed.
References
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Journal ArticleDOI

Animal cell cycles and their control

TL;DR: The search for an S Phase-Promoting Factor and the regulation of p34cdc2 Activity by Phosphorylation are explored.
Journal ArticleDOI

DNA excision repair

TL;DR: Transcribed strands are specifically targeted for excision repair by a transcription-repair coupling factor both in E. coli and in humans, which is an important defense mechanism against the two major carcinogens, sunlight and cigarette smoke.
Journal ArticleDOI

Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein

TL;DR: The RAD51 gene of Saccharomyces cerevisiae is required for genetic recombination and DNA double-strand break repair and it is demonstrated that RAD51 protein pairs circular viral single-stranded DNA from phi X 174 or M13 with its respective homologous linear double-Stranded form, indicating that RAD 51 can catalyze strand exchange.
Journal ArticleDOI

Defective DNA-dependent protein kinase activity is linked to V(D)J recombination and DNA repair defects associated with the murine scid mutation

TL;DR: It is demonstrated that yeast artificial chromosomes containing the DNA- PKcs gene complement both the DNA repair and recombination deficiencies of V3 cells, and it is concluded that DNA-PKcs is encoded by the XRCC7 gene.
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