Replication and nicking of zygotene DNA sequences. Control by a meiosis-specific protein

A protein having a molecular weight of 73,000 daltons has been purified from the nuclear membranes of preleptotene, leptotene, and zygotene cells. It has been named the leptotene protein (L-protein) because of its role in suppressing the replication of zygotene DNA sequences through leptotene until the initiation of zygotene DNA synthesis. The protein has been found to be highly specific in its inhibitory activity. S-phase replication in somatic nuclei and in microspore nuclei are unaffected by the protein. Only zygotene DNA sequences appear to be affected. L-protein binds specifically to zygotene DNA. The binding is limited to a relatively short DNA segment, probably no longer than 90 base pairs (bp). Chloroplast and mitochondrial DNA do not bind to the protein, but a low level of binding is displayed by DNA from several other eukaryotic species. The L-protein also has the capacity to nick the bound DNA in the presence of ATP. Nicking does not occur in the absence of binding. Using supercoiled plasmids with zygotene DNA inserts as substrates, the nicking has been found to be confined to a small region of the plasmid and to occur in only one of the strands. The L-protein is considered to be one of the principal factors responsible for the irreversible commitment of cells to meiosis at the end of the preleptotene S-phase. It is also proposed that its endonucleolytic activity plays a role in the initiation of synapsis.