Mms21 SUMO Ligase Activity Promotes Nucleolar Function in Saccharomyces cerevisiae
Author(s) -
DongHwan Kim,
Bethany D. Harris,
Fei Wang,
Chris Seidel,
Scott McCroskey,
Jennifer L. Gerton
Publication year - 2016
Publication title -
genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.792
H-Index - 246
eISSN - 1943-2631
pISSN - 0016-6731
DOI - 10.1534/genetics.115.181750
Subject(s) - biology , ribosome biogenesis , mutant , genetics , microbiology and biotechnology , establishment of sister chromatid cohesion , dna repair , saccharomyces cerevisiae , ribosome , ubiquitin ligase , ribosomal protein , rna , gene , ubiquitin , cohesin , meiosis
The budding yeast E3 SUMO ligase Mms21, also known as Nse2, is a component of the Smc5/6 complex, which regulates sister chromatid cohesion, DNA replication, and repair. Our study shows that the mms21RINGΔ mutant exhibits (1) reduced ribosomal RNA production; (2) nuclear accumulation of ribosomal proteins; (3) elevated Gcn4 translation, indicating translational stress; and (4) upregulation of Gcn4 targets. Genes involved in ribosome biogenesis and translation are downregulated in the mms21RINGΔ mutant. We identified RPL19A as a novel genetic suppressor of the mms21RINGΔ mutant. Deletion of RPL19A partially suppresses growth defects in both smc5-6 and mms21RINGΔ mutants as well as nuclear accumulation of ribosome subunits in the mms21RINGΔ mutant. Deletion of a previously identified strong suppressor, MPH1, rescues both the accumulation of ribosome subunits and translational stress. This study suggests that the Smc5/6 complex supports nucleolar function.
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