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 doublestrand
break formation. Moreover, the proportion of Zip1
polycomplexes, which indicate abnormal SC formation, in
cells with a mutation in UBI4 (i.e., ubi4Δ 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
ubi4Δ 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, ubi4Δ cells proficiently form crossover
and noncrossover products with a slight delay compared
to wild-type cells, suggesting that UBI4 is dispensable in SCcoupled
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.