Cooperation of sumoylated chromosomal proteins in rDNA maintenance.

SUMO is a posttranslational modifier that can modulate protein activities, interactions, and localizations. As the GFP-Smt3p fusion protein has a preference for subnucleolar localization, especially when deconjugation is impaired, the nucleolar role of SUMO can be the key to its biological functions...

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Main Authors: Yoshimitsu Takahashi, Stanimir Dulev, Xianpeng Liu, Natalie Jasmin Hiller, Xiaolan Zhao, Alexander Strunnikov
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2008-10-01
Series:PLoS Genetics
Online Access:http://europepmc.org/articles/PMC2563031?pdf=render
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author Yoshimitsu Takahashi
Stanimir Dulev
Xianpeng Liu
Natalie Jasmin Hiller
Xiaolan Zhao
Alexander Strunnikov
author_facet Yoshimitsu Takahashi
Stanimir Dulev
Xianpeng Liu
Natalie Jasmin Hiller
Xiaolan Zhao
Alexander Strunnikov
author_sort Yoshimitsu Takahashi
collection DOAJ
description SUMO is a posttranslational modifier that can modulate protein activities, interactions, and localizations. As the GFP-Smt3p fusion protein has a preference for subnucleolar localization, especially when deconjugation is impaired, the nucleolar role of SUMO can be the key to its biological functions. Using conditional triple SUMO E3 mutants, we show that defects in sumoylation impair rDNA maintenance, i.e., the rDNA segregation is defective and the rDNA copy number decreases in these mutants. Upon characterization of sumoylated proteins involved in rDNA maintenance, we established that Top1p and Top2p, which are sumoylated by Siz1p/Siz2p, most likely collaborate with substrates of Mms21p to maintain rDNA integrity. Cohesin and condensin subunits, which both play important roles in rDNA stability and structures, are potential substrates of Mms21, as their sumoylation depends on Mms21p, but not Siz1p and Siz2p. In addition, binding of cohesin and condensin to rDNA is altered in the mms21-CH E3-deficient mutant.
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spelling doaj.art-f993b86744f14f59ae2bfc8d9216eecc2022-12-21T23:15:58ZengPublic Library of Science (PLoS)PLoS Genetics1553-73901553-74042008-10-01410e100021510.1371/journal.pgen.1000215Cooperation of sumoylated chromosomal proteins in rDNA maintenance.Yoshimitsu TakahashiStanimir DulevXianpeng LiuNatalie Jasmin HillerXiaolan ZhaoAlexander StrunnikovSUMO is a posttranslational modifier that can modulate protein activities, interactions, and localizations. As the GFP-Smt3p fusion protein has a preference for subnucleolar localization, especially when deconjugation is impaired, the nucleolar role of SUMO can be the key to its biological functions. Using conditional triple SUMO E3 mutants, we show that defects in sumoylation impair rDNA maintenance, i.e., the rDNA segregation is defective and the rDNA copy number decreases in these mutants. Upon characterization of sumoylated proteins involved in rDNA maintenance, we established that Top1p and Top2p, which are sumoylated by Siz1p/Siz2p, most likely collaborate with substrates of Mms21p to maintain rDNA integrity. Cohesin and condensin subunits, which both play important roles in rDNA stability and structures, are potential substrates of Mms21, as their sumoylation depends on Mms21p, but not Siz1p and Siz2p. In addition, binding of cohesin and condensin to rDNA is altered in the mms21-CH E3-deficient mutant.http://europepmc.org/articles/PMC2563031?pdf=render
spellingShingle Yoshimitsu Takahashi
Stanimir Dulev
Xianpeng Liu
Natalie Jasmin Hiller
Xiaolan Zhao
Alexander Strunnikov
Cooperation of sumoylated chromosomal proteins in rDNA maintenance.
PLoS Genetics
title Cooperation of sumoylated chromosomal proteins in rDNA maintenance.
title_full Cooperation of sumoylated chromosomal proteins in rDNA maintenance.
title_fullStr Cooperation of sumoylated chromosomal proteins in rDNA maintenance.
title_full_unstemmed Cooperation of sumoylated chromosomal proteins in rDNA maintenance.
title_short Cooperation of sumoylated chromosomal proteins in rDNA maintenance.
title_sort cooperation of sumoylated chromosomal proteins in rdna maintenance
url http://europepmc.org/articles/PMC2563031?pdf=render
work_keys_str_mv AT yoshimitsutakahashi cooperationofsumoylatedchromosomalproteinsinrdnamaintenance
AT stanimirdulev cooperationofsumoylatedchromosomalproteinsinrdnamaintenance
AT xianpengliu cooperationofsumoylatedchromosomalproteinsinrdnamaintenance
AT nataliejasminhiller cooperationofsumoylatedchromosomalproteinsinrdnamaintenance
AT xiaolanzhao cooperationofsumoylatedchromosomalproteinsinrdnamaintenance
AT alexanderstrunnikov cooperationofsumoylatedchromosomalproteinsinrdnamaintenance