Changes in protein composition of meiotic nodules during mammalian meiosis.
Homologous chromosome synapsis and meiotic recombination are facilitated by several meiosis-specific structures: the synaptonemal complex (SC), and two types of meiotic nodules: (1) early meiotic nodules (MNs), also called zygotene nodules or early recombination nodules, and (2) late recombination nodules (RNs). The former are thought to be nucleoprotein complexes involved in the check for homology preceding, or accompanying synapsis, while the latter have been shown to be involved in reciprocal recombination. We have examined by immunocytochemistry the meiotic localization of a series of proteins at sites along the asynapsed axial elements prior to homologous synapsis and at sites along the SCs following synapsis. Several of the proteins examined have been implicated in repair/recombination and include RAD51, a mammalian homolog of the Escherichia coli RecA protein; Replication Protein-A (RPA), a single-strand DNA binding protein; and MLH1, a mismatch repair protein which is a homolog of the E. coli MutL protein. In addition two proteins were examined that have been implicated in meiotic checkpoints: ATM, the protein mutated in the human disease Ataxia Telangiectasia, and ATR, another member of the same family of PIK kinases. We present evidence that these proteins are all components of meiotic nodules and document changes in protein composition of these structures during zygonema and pachynema of meiotic prophase in mouse spermatocytes. These studies support the supposition that a subset of MNs are converted into RNs. However, our data also demonstrate changes in protein composition within the context of early MNs, suggesting a differentiation of these nodules during the process of synapsis. The same changes in protein composition occurred on both the normal X axis, which has no homologous pairing partner in spermatocytes, and on the axes of aberrant chromosomes that nonhomologously synapse during synaptic adjustment. These findings suggest that DNA sequences associated with MNs still must undergo an obligatory processing, even in the absence of interactions between homologous chromosomes.
Plug
A W
AW
Department of Genetics, Yale University School of Medicine, New Haven, CT 06510, USA.
Peters
A H
AH
Keegan
K S
KS
Hoekstra
M F
MF
de Boer
P
P
Ashley
T
T
D000818:Animals; D064007:Ataxia Telangiectasia Mutated Proteins; D018797:Cell Cycle Proteins / Q000032:analysis; D002875:Chromosomes / Q000737:chemistry; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000032:analysis*; D008297:Male; D008540:Meiosis; D051379:Mice; D008807:Mice, Inbred BALB C; D009698:Nucleoproteins / Q000737:chemistry*; D017346:Protein Serine-Threonine Kinases; D011506:Proteins / Q000032:analysis*; D051135:Rad51 Recombinase; D011995:Recombination, Genetic; D051716:Replication Protein A; D013090:Spermatocytes; D014178:Translocation, Genetic; D025521:Tumor Suppressor Proteins
D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; D009698:Nucleoproteins; D011506:Proteins; D051716:Replication Protein A; C497168:Rpa1 protein, mouse; D025521:Tumor Suppressor Proteins; C576897:Atr protein, mouse; C576324:ATM protein, human; D064007:Ataxia Telangiectasia Mutated Proteins; C576325:Atm protein, mouse; D017346:Protein Serine-Threonine Kinases; D051135:Rad51 Recombinase; C495154:Rad51 protein, mouse