PMID- 10562567
OWN - NLM
STAT- MEDLINE
DCOM- 20000120
LR  - 20081120
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 22
DP  - 1999 Nov 15
TI  - The meiosis-specific recombinase hDmc1 forms ring structures and interacts with
      hRad51.
PG  - 6552-60
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.
FAU - Masson, J Y
AU  - Masson JY
AD  - Imperial Cancer Research Fund, Clare Hall Laboratories, South Mimms,
      Hertfordshire EN6 3LD, UK.
FAU - Davies, A A
AU  - Davies AA
FAU - Hajibagheri, N
AU  - Hajibagheri N
FAU - Van Dyck, E
AU  - Van Dyck E
FAU - Benson, F E
AU  - Benson FE
FAU - Stasiak, A Z
AU  - Stasiak AZ
FAU - Stasiak, A
AU  - Stasiak A
FAU - West, S C
AU  - West SC
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (DNA, Single-Stranded)
RN  - 0 (DNA, Viral)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Nucleic Acid Heteroduplexes)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Recombinases)
RN  - EC 2.7.7.- (DNA Nucleotidyltransferases)
RN  - EC 2.7.7.- (Integrases)
RN  - EC 2.7.7.- (RAD51 protein, human)
RN  - EC 2.7.7.- (Rad51 Recombinase)
RN  - EC 2.7.7.- (Rec A Recombinases)
RN  - EC 2.7.7.- (integron integrase IntI1)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
RN  - EC 3.6.1.- (DMC1 protein, human)
SB  - IM
MH  - Adenosine Triphosphatases/isolation & purification/*metabolism/*ultrastructure
MH  - *Cell Cycle Proteins
MH  - Cloning, Molecular
MH  - DNA Nucleotidyltransferases/isolation & purification/*metabolism/*ultrastructure
MH  - DNA, Single-Stranded/biosynthesis/chemistry
MH  - DNA, Viral/biosynthesis/chemistry
MH  - DNA-Binding Proteins/*chemistry/isolation &
      purification/*metabolism/*ultrastructure
MH  - Escherichia coli/genetics
MH  - Gene Library
MH  - Humans
MH  - *Integrases
MH  - Male
MH  - Meiosis
MH  - Microscopy, Electron
MH  - Nucleic Acid Heteroduplexes/biosynthesis/chemistry
MH  - Organ Specificity
MH  - Rad51 Recombinase
MH  - Rec A Recombinases/metabolism
MH  - Recombinant Proteins/chemistry/metabolism/ultrastructure
MH  - Recombinases
MH  - Recombination, Genetic
MH  - Testis/enzymology
PMC - PMC1171718
EDAT- 1999/11/24 00:00
MHDA- 1999/11/24 00:01
CRDT- 1999/11/24 00:00
PHST- 1999/11/24 00:00 [pubmed]
PHST- 1999/11/24 00:01 [medline]
PHST- 1999/11/24 00:00 [entrez]
AID - 10.1093/emboj/18.22.6552 [doi]
PST - ppublish
SO  - EMBO J. 1999 Nov 15;18(22):6552-60. doi: 10.1093/emboj/18.22.6552.