Journal
NUCLEIC ACIDS RESEARCH
Volume 42, Issue 2, Pages 906-917Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkt924
Keywords
-
Categories
Funding
- US National Institutes of Health [RO1ES015252, RO1CA168635, RO1ES007061, PO1CA092584]
- National Science Council of Taiwan [NSC 99-2311-B-002-012, NSC 100-2311-B-002-009]
- National Basic Research Program of China [2010CB912401]
- National Center for Protein Sciences Beijing
- NATIONAL CANCER INSTITUTE [P01CA092584, R01CA168635] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [ZIADK052033] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES [R01ES007061, R01ES015252] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P20GM103636, R01GM105404] Funding Source: NIH RePORTER
Ask authors/readers for more resources
The Hop2-Mnd1 complex functions with the DMC1 recombinase in meiotic recombination. Hop2-Mnd1 stabilizes the DMC1-single-stranded DNA (ssDNA) filament and promotes the capture of the double-stranded DNA partner by the recombinase filament to assemble the synaptic complex. Herein, we define the action mechanism of Hop2-Mnd1 in DMC1-mediated recombination. Small angle X-ray scattering analysis and electron microscopy reveal that the heterodimeric Hop2-Mnd1 is a V-shaped molecule. We show that the protein complex harbors three distinct DNA binding sites, and determine their functional relevance. Specifically, the N-terminal double-stranded DNA binding functions of Hop2 and Mnd1 co-operate to mediate synaptic complex assembly, whereas ssDNA binding by the Hop2 C-terminus helps stabilize the DMC1-ssDNA filament. A model of the Hop2-Mnd1-DMC1-ssDNA ensemble is proposed to explain how it mediates homologous DNA pairing in meiotic recombination.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available
Share Paper
