Yeast polyubiquitin unit regulates synaptonemal complex formation and recombination during meiosis

Abstract

Ubiquitin is highly conserved in most eukaryotes and involved in diverse physiological processes, including cell division, protein quality control, and protein degradation mediated by the ubiquitin-proteasome system after heat shock, glucose-starvation, and oxidative stress. However, the role of the ubiquitin gene UBI4, which contains five consecutive head-to-tail ubiquitin repeats, in meiosis has not been investigated. In this study, we show that the Saccharomyces cerevisiae polyubiquitin precursor gene, UBI4, is required to promote synaptonemal complex (SC) formation and suppress excess double-strand break formation. Moreover, the proportion of Zip1 polycomplexes, which indicate abnormal SC formation, in cells with a mutation in UBI4 (i.e., ubi4 Delta cells) is higher than that of wild-type cells, implying that the UBI4 plays an important role in the early meiotic prophase I. Interestingly, although ubi4 Delta cells rarely form full-length SCs in the pachytene stage of prophase I, the Zip3 foci are still seen, as in wild-type cells. Moreover, ubi4 Delta cells proficiently form crossover and noncrossover products with a slight delay compared to wild-type cells, suggesting that UBI4 is dispensable in SC-coupled recombination. Our findings demonstrate that UBI4 exhibits dual functions that are associated with both positive and negative roles in SC formation and recombination during meiosis.