cooperation of sumoylated chromosomal proteins in rdna maintenance合作sumoylated染色体蛋白质rdna维护.pdfVIP

Cooperation of Sumoylated Chromosomal Proteins in rDNA Maintenance 1 1,2 3 4¤ 3 Yoshimitsu Takahashi , Stanimir Dulev , Xianpeng Liu , Natalie Jasmin Hiller , Xiaolan Zhao , Alexander Strunnikov1* 1 Laboratory of Gene Regulation and Development, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland, United States of America, 2 University of Plovdiv, Plovdiv, Bulgaria, 3 Molecular Biology Department, Memorial Sloan Kettering Institute, New York, New York, United States of America, 4 The Rockefeller University, New York, New York, United States of America Abstract 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. Citation: Takahashi Y, Dulev S, Liu X, Hiller NJ, Zhao X,