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RPA complexes in Caenorhabditis elegans meiosis; unique roles in replication, meiotic recombination and apoptosis.
- Source :
-
Nucleic acids research [Nucleic Acids Res] 2021 Feb 26; Vol. 49 (4), pp. 2005-2026. - Publication Year :
- 2021
-
Abstract
- Replication Protein A (RPA) is a critical complex that acts in replication and promotes homologous recombination by allowing recombinase recruitment to processed DSB ends. Most organisms possess three RPA subunits (RPA1, RPA2, RPA3) that form a trimeric complex critical for viability. The Caenorhabditis elegans genome encodes RPA-1, RPA-2 and an RPA-2 paralog RPA-4. In our analysis, we determined that RPA-2 is critical for germline replication and normal repair of meiotic DSBs. Interestingly, RPA-1 but not RPA-2 is essential for somatic replication, in contrast to other organisms that require both subunits. Six different hetero- and homodimeric complexes containing permutations of RPA-1, RPA-2 and RPA-4 can be detected in whole animal extracts. Our in vivo studies indicate that RPA-1/4 dimer is less abundant in the nucleus and its formation is inhibited by RPA-2. While RPA-4 does not participate in replication or recombination, we find that RPA-4 inhibits RAD-51 filament formation and promotes apoptosis of a subset of damaged nuclei. Altogether these findings point to sub-functionalization and antagonistic roles of RPA complexes in C. elegans.<br /> (© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.)
- Subjects :
- Animals
Caenorhabditis elegans Proteins analysis
Caenorhabditis elegans Proteins metabolism
DNA Breaks, Double-Stranded
Mitosis genetics
Rad51 Recombinase analysis
Replication Protein A metabolism
Apoptosis
Caenorhabditis elegans genetics
Caenorhabditis elegans Proteins physiology
DNA Replication
Meiosis genetics
Recombination, Genetic
Replication Protein A physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1362-4962
- Volume :
- 49
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Nucleic acids research
- Publication Type :
- Academic Journal
- Accession number :
- 33476370
- Full Text :
- https://doi.org/10.1093/nar/gkaa1293