Abstract
RecA-like proteins have been purified from somatic and meiotic cells of mouse and lily. The rec proteins have been designated “s-rec” and “m-rec” to indicate their respective tissues of origin. The two proteins differ in molecular weight and in their response to temperature, the latter being consistent with the optimal temperature for physiological function of their tissues of origin. There is a major increase in m-rec protein with the entry of cells into meiosis, the peak of activity being early pachytene. Extracts of the cells and also those of yeast (Saccharomyces cerevisiae) have been prepared that have the capacity to catalyze homologous recombination. These extracts behave similarly to the m-rec proteins upon entry of cells into meiosis. Yeast transferred to sporulation medium displays a 100-fold increase in the recombination activity of the extract at about the time of entry into meiosis. The occurrence of peak levels of m-rec and recombination activity in extracts from cells in early pachytene points strongly to that stage as the time at which the enzymatic phase of recombination occurs.
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Hotta, Y., Tabata, S., Bouchard, R.A. et al. General recombination mechanisms in extracts of meiotic cells. Chromosoma 93, 140–151 (1985). https://doi.org/10.1007/BF00293161
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DOI: https://doi.org/10.1007/BF00293161