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Replication Protein A and Sex: What's Phosphorylation Got To Do With It?
Author(s) -
Wilson Timothy M.,
Piya Gunjan,
Haring Stuart J.
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.937.1
Subject(s) - meiosis , homologous recombination , biology , dna replication , chromosome segregation , microbiology and biotechnology , homologous chromosome , replication protein a , heterotrimeric g protein , phosphorylation , origin recognition complex , mitosis , ploidy , dna damage , genetics , replication factor c , g2 m dna damage checkpoint , dna repair , cell cycle , dna , control of chromosome duplication , eukaryotic dna replication , chromosome , dna binding protein , cell cycle checkpoint , cell , gene , signal transduction , transcription factor , g protein
Meiosis is an essential part of sexual reproduction that is required to create viable haploid gametes from diploid parental cells. A unique feature of meiosis is the programmed exchange of genetic information through homologous recombination (HR), which is also essential for the proper segregation of chromosomes during the reductional division. Replication Protein A (RPA) is a heterotrimeric protein complex conserved amongst all eukaryotes that binds single‐stranded DNA (ssDNA) and participates in DNA replication, repair, cell cycle regulation, and HR. Interestingly, the N‐terminus of the Rfa2 subunit is hyper‐phosphorylated in response to DNA damage. Rfa2 is also phosphorylated during meiosis by a meiosis‐specific kinase (Ime2) and by a damage‐inducible checkpoint kinase (Mec1). Our goal is to understand the role of Rfa2 N‐terminal phosphorylation in meiosis. To do this, we have generated phospho‐mimetic and non‐phosphorylatable Rfa2 mutants. These mutants show DNA damage‐dependent sensitivities in mitotic cells, and the importance of the phosphorylation state of Rfa2 in meiotic cells is being examined. This work is supported through funds provided by Chemistry and Biochemistry (NDSU) to SJH.