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Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere maintenance
Author(s) -
Xhemalce Blerta,
Seeler JacobS,
Thon Geneviève,
Dejean Anne,
Arcangioli Benoît
Publication year - 2004
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600394
Subject(s) - biology , schizosaccharomyces , minichromosome , telomere , heterochromatin , sumo protein , centromere , genetics , schizosaccharomyces pombe , microbiology and biotechnology , gene silencing , ubiquitin ligase , saccharomyces cerevisiae , gene , chromosome , ubiquitin
Sumoylation represents a conserved mechanism of post‐translational protein modification. We report that Pli1p, the unique fission yeast member of the SP‐RING family, is a SUMO E3 ligase in vivo and in vitro . pli1 Δ cells display no obvious mitotic growth defects, but are sensitive to the microtubule‐destabilizing drug TBZ and exhibit enhanced minichromosome loss. The weakened centromeric function of pli1 Δ cells may be related to the defective heterochromatin structure at the central core, as shown by the reduced silencing of an ura4 variegation reporter gene inserted at cnt and imr . Interestingly, pli1 Δ cells also exhibit enhanced loss of the ura4 reporter at these loci, likely by gene conversion using homologous sequences as information donors. Moreover, pli1 Δ cells exhibit consistent telomere length increase, possibly achieved by a similar process. Point mutations within the RING finger of Pli1p totally or partially reproduce the pli1 deletion phenotypes, thus correlating with their sumoylation activity. Altogether, these results strongly suggest that Pli1p, and by extension sumoylation, is involved in mechanisms that regulate recombination in particular heterochromatic repeated sequences.