Home > Research > Publications & Outputs > The meiosis-specific recombinase hDmc1 forms ri...
View graph of relations

The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Published

Standard

The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51. / Masson, J. Y.; Davies, A. A.; Hajibagheri, N. et al.
In: EMBO Journal, Vol. 18, No. 22, 11.1999, p. 6552-6560.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Masson, JY, Davies, AA, Hajibagheri, N, Van Dyck, E, Benson, FE, Stasiak, AZ, Stasiak, A & West, SC 1999, 'The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51.', EMBO Journal, vol. 18, no. 22, pp. 6552-6560. https://doi.org/10.1093/emboj/18.22.6552

APA

Masson, J. Y., Davies, A. A., Hajibagheri, N., Van Dyck, E., Benson, F. E., Stasiak, A. Z., Stasiak, A., & West, S. C. (1999). The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51. EMBO Journal, 18(22), 6552-6560. https://doi.org/10.1093/emboj/18.22.6552

Vancouver

Masson JY, Davies AA, Hajibagheri N, Van Dyck E, Benson FE, Stasiak AZ et al. The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51. EMBO Journal. 1999 Nov;18(22):6552-6560. doi: 10.1093/emboj/18.22.6552

Author

Masson, J. Y. ; Davies, A. A. ; Hajibagheri, N. et al. / The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51. In: EMBO Journal. 1999 ; Vol. 18, No. 22. pp. 6552-6560.

Bibtex

@article{45b26788e60f44cc966b35d378c7baac,
title = "The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51.",
abstract = "Eukaryotic cells encode two homologs of Escherichia coli RecA protein, Rad51 and Dmc1, which are required for meiotic recombination. Rad51, like E.coli RecA, forms helical nucleoprotein filaments that promote joint molecule and heteroduplex DNA formation. Electron microscopy reveals that the human meiosis-specific recombinase Dmc1 forms ring structures that bind single-stranded (ss) and double-stranded (ds) DNA. The protein binds preferentially to ssDNA tails and gaps in duplex DNA. hDmc1–ssDNA complexes exhibit an irregular, often compacted structure, and promote strand-transfer reactions with homologous duplex DNA. hDmc1 binds duplex DNA with reduced affinity to form nucleoprotein complexes. In contrast to helical RecA/Rad51 filaments, however, Dmc1 filaments are composed of a linear array of stacked protein rings. Consistent with the requirement for two recombinases in meiotic recombination, hDmc1 interacts directly with hRad51.",
keywords = "hDmc1, hRad51, meiotic recombination, recombinases, ring structures",
author = "Masson, {J. Y.} and Davies, {A. A.} and N. Hajibagheri and {Van Dyck}, E. and Benson, {Fiona E.} and Stasiak, {A. Z.} and A. Stasiak and West, {S. C.}",
year = "1999",
month = nov,
doi = "10.1093/emboj/18.22.6552",
language = "English",
volume = "18",
pages = "6552--6560",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Nature Publishing Group",
number = "22",

}

RIS

TY - JOUR

T1 - The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51.

AU - Masson, J. Y.

AU - Davies, A. A.

AU - Hajibagheri, N.

AU - Van Dyck, E.

AU - Benson, Fiona E.

AU - Stasiak, A. Z.

AU - Stasiak, A.

AU - West, S. C.

PY - 1999/11

Y1 - 1999/11

N2 - Eukaryotic cells encode two homologs of Escherichia coli RecA protein, Rad51 and Dmc1, which are required for meiotic recombination. Rad51, like E.coli RecA, forms helical nucleoprotein filaments that promote joint molecule and heteroduplex DNA formation. Electron microscopy reveals that the human meiosis-specific recombinase Dmc1 forms ring structures that bind single-stranded (ss) and double-stranded (ds) DNA. The protein binds preferentially to ssDNA tails and gaps in duplex DNA. hDmc1–ssDNA complexes exhibit an irregular, often compacted structure, and promote strand-transfer reactions with homologous duplex DNA. hDmc1 binds duplex DNA with reduced affinity to form nucleoprotein complexes. In contrast to helical RecA/Rad51 filaments, however, Dmc1 filaments are composed of a linear array of stacked protein rings. Consistent with the requirement for two recombinases in meiotic recombination, hDmc1 interacts directly with hRad51.

AB - Eukaryotic cells encode two homologs of Escherichia coli RecA protein, Rad51 and Dmc1, which are required for meiotic recombination. Rad51, like E.coli RecA, forms helical nucleoprotein filaments that promote joint molecule and heteroduplex DNA formation. Electron microscopy reveals that the human meiosis-specific recombinase Dmc1 forms ring structures that bind single-stranded (ss) and double-stranded (ds) DNA. The protein binds preferentially to ssDNA tails and gaps in duplex DNA. hDmc1–ssDNA complexes exhibit an irregular, often compacted structure, and promote strand-transfer reactions with homologous duplex DNA. hDmc1 binds duplex DNA with reduced affinity to form nucleoprotein complexes. In contrast to helical RecA/Rad51 filaments, however, Dmc1 filaments are composed of a linear array of stacked protein rings. Consistent with the requirement for two recombinases in meiotic recombination, hDmc1 interacts directly with hRad51.

KW - hDmc1

KW - hRad51

KW - meiotic recombination

KW - recombinases

KW - ring structures

U2 - 10.1093/emboj/18.22.6552

DO - 10.1093/emboj/18.22.6552

M3 - Journal article

VL - 18

SP - 6552

EP - 6560

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 22

ER -