Journal article
The dual role of HOP2 in mammalian meiotic homologous recombination
Nucleic acids research, v 42(4), pp 2346-2357
Feb 2014
PMID: 24304900
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Deletion of
Hop2
in mice eliminates homologous chromosome synapsis and disrupts double-strand break (DSB) repair through homologous recombination. HOP2
in vitro
shows two distinctive activities: when it is incorporated into a HOP2–MND1 complex it stimulates DMC1 and RAD51 recombination activities and the purified HOP2 alone is proficient in promoting strand invasion. We observed that a fraction of
Mnd1
−/−
spermatocytes, which express HOP2 but apparently have inactive DMC1 and RAD51 due to lack of the HOP2–MND1 complex, exhibits a high level of chromosome synapsis and that most DSBs in these spermatocytes are repaired. This suggests that DSB repair catalyzed solely by HOP2 supports homologous chromosome pairing and synapsis. In addition, we show that
in vitro
HOP2 promotes the co-aggregation of ssDNA with duplex DNA, binds to ssDNA leading to unstacking of the bases, and promotes the formation of a three-strand synaptic intermediate. However, HOP2 shows distinctive mechanistic signatures as a recombinase. Namely, HOP2-mediated strand exchange does not require ATP and, in contrast to DMC1, joint molecules formed by HOP2 are more sensitive to mismatches and are efficiently dissociated by RAD54. We propose that HOP2 may act as a recombinase with specific functions in meiosis.
Metrics
Details
- Title
- The dual role of HOP2 in mammalian meiotic homologous recombination
- Creators
- Roberto J Pezza - Oklahoma Medical Research Foundation, Oklahoma City, 73104 OK, USAOleg N Voloshin - Oklahoma Medical Research Foundation, Oklahoma City, 73104 OK, USAAlexander A Volodin - Oklahoma Medical Research Foundation, Oklahoma City, 73104 OK, USAKingsley A Boateng - Oklahoma Medical Research Foundation, Oklahoma City, 73104 OK, USAMarina A Bellani - Oklahoma Medical Research Foundation, Oklahoma City, 73104 OK, USAAlexander V Mazin - Oklahoma Medical Research Foundation, Oklahoma City, 73104 OK, USAR. Daniel Camerini-Otero - Oklahoma Medical Research Foundation, Oklahoma City, 73104 OK, USA
- Publication Details
- Nucleic acids research, v 42(4), pp 2346-2357
- Publisher
- Oxford University Press
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000332381000029
- Scopus ID
- 2-s2.0-84895802706
- Other Identifier
- 991014877662904721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology