PMID- 10525529
OWN - NLM
STAT- MEDLINE
DCOM- 19991117
LR  - 20191210
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 147
IP  - 2
DP  - 1999 Oct 18
TI  - RAD51 and DMC1 form mixed complexes associated with mouse meiotic chromosome
      cores and synaptonemal complexes.
PG  - 207-20
AB  - The eukaryotic RecA homologues RAD51 and DMC1 function in homology recognition
      and formation of joint-molecule recombination intermediates during yeast meiosis.
      The precise immunolocalization of these two proteins on the meiotic chromosomes
      of plants and animals has been complicated by their high degree of identity at
      the amino acid level. With antibodies that have been immunodepleted of
      cross-reactive epitopes, we demonstrate that RAD51 and DMC1 have identical
      distribution patterns in extracts of mouse spermatocytes in successive prophase I
      stages, suggesting coordinate functionality. Immunofluorescence and
      immunoelectron microscopy with these antibodies demonstrate colocalization of the
      two proteins on the meiotic chromosome cores at early prophase I. We also show
      that mouse RAD51 and DMC1 establish protein-protein interactions with each other 
      and with the chromosome core component COR1(SCP3) in a two-hybrid system and in
      vitro binding analyses. These results suggest that the formation of a
      multiprotein recombination complex associated with the meiotic chromosome cores
      is essential for the development and fulfillment of the meiotic recombination
      process.
FAU - Tarsounas, M
AU  - Tarsounas M
AD  - Department of Biology, York University, 4700 Keele Street, Toronto, Ontario M3J
      1P3, Canada.
FAU - Morita, T
AU  - Morita T
FAU - Pearlman, R E
AU  - Pearlman RE
FAU - Moens, P B
AU  - Moens PB
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Dmc1 protein, mouse)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphate-Binding Proteins)
RN  - EC 2.7.7.- (Rad51 Recombinase)
RN  - EC 2.7.7.- (Rad51 protein, mouse)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
SB  - IM
MH  - *Adenosine Triphosphatases
MH  - Animals
MH  - *Cell Cycle Proteins
MH  - DNA-Binding Proteins/*genetics
MH  - Immunohistochemistry
MH  - Male
MH  - Meiosis/*genetics
MH  - Mice
MH  - Nuclear Proteins
MH  - Phosphate-Binding Proteins
MH  - Rad51 Recombinase
MH  - *Recombination, Genetic
MH  - Spermatocytes/cytology/*physiology
PMC - PMC2174216
EDAT- 1999/10/20 00:00
MHDA- 1999/10/20 00:01
CRDT- 1999/10/20 00:00
PHST- 1999/10/20 00:00 [pubmed]
PHST- 1999/10/20 00:01 [medline]
PHST- 1999/10/20 00:00 [entrez]
AID - 10.1083/jcb.147.2.207 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Oct 18;147(2):207-20. doi: 10.1083/jcb.147.2.207.