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Condensin but not cohesin SMC heterodimer induces DNA reannealing through protein–protein assembly
Author(s) -
Sakai Akiko,
Hizume Kohji,
Sutani Takashi,
Takeyasu Kunio,
Yanagida Mitsuhiro
Publication year - 2003
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 - 10.1093/emboj/cdg247
Subject(s) - condensin , cohesin , establishment of sister chromatid cohesion , biology , chromosome segregation , dna , microbiology and biotechnology , chromatid , sister chromatids , chromatin , chromosome , genetics , gene
Condensin and cohesin are chromosomal protein complexes required for chromosome condensation and sister chromatid cohesion, respectively. They commonly contain the SMC ( s tructural m aintenance of c hromosomes) subunits consisting of a long coiled‐coil with the terminal globular domains and the central hinge. Condensin and cohesin holo‐complexes contain three and two non‐SMC subunits, respectively. In this study, DNA interaction with cohesin and condensin complexes purified from fission yeast was investigated. The DNA reannealing activity is strong for condensin SMC heterodimer but weak for holo‐condensin, whereas no annealing activity is found for cohesin heterodimer SMC and Rad21‐bound heterotrimer complexes. One set of globular domains of the same condensin SMC is essential for the DNA reannealing activity. In addition, the coiled‐coil and hinge region of another SMC are needed. Atomic force microscopy discloses the molecular events of DNA reannealing. SMC assembly that occurs on reannealing DNA seems to be a necessary intermediary step. SMC is eliminated from the completed double‐stranded DNA. The ability of heterodimeric SMC to reanneal DNA may be regulated in vivo possibly through the non‐SMC heterotrimeric complex.