title: ATPase-dependent auto-phosphorylation of the open condensin hinge diminishes DNA binding.
abstract: Condensin, which contains two structural maintenance of chromosome (SMC) subunits and three regulatory non-SMC subunits, is essential for many chromosomal functions, including mitotic chromosome condensation and segregation. The ATPase domain of the SMC subunit comprises two termini connected by a long helical domain that is interrupted by a central hinge. The role of the ATPase domain has remained elusive. Here we report that the condensin SMC subunit of the fission yeast Schizosaccharomyces pombe is phosphorylated in a manner that requires the presence of the intact SMC ATPase Walker motif. Principal phosphorylation sites reside in the conserved, glycine-rich stretch at the hinge interface surrounded by the highly basic DNA-binding patch. Phosphorylation reduces affinity for DNA. Consistently, phosphomimetic mutants produce severe mitotic phenotypes. Structural evidence suggests that prior opening (though slight) of the hinge is necessary for phosphorylation, which is implicated in condensin's dissociation from and its progression along DNA.
authors.affiliation: Okinawa Institute of Science and Technology Graduate University, Onna-son, Okinawa 904-0495, Japan.
authors.forename: Yuko
authors.initials: Y
authors.lastname: Akai
authors.affiliation: Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan.
authors.forename: Ryuta
authors.initials: R
authors.lastname: Kanai
authors.affiliation: Okinawa Institute of Science and Technology Graduate University, Onna-son, Okinawa 904-0495, Japan.
authors.forename: Norihiko
authors.initials: N
authors.lastname: Nakazawa
authors.affiliation: Okinawa Institute of Science and Technology Graduate University, Onna-son, Okinawa 904-0495, Japan.
authors.forename: Masahiro
authors.initials: M
authors.lastname: Ebe
authors.affiliation: Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan.
authors.forename: Chikashi
authors.initials: C
authors.lastname: Toyoshima
authors.affiliation: Okinawa Institute of Science and Technology Graduate University, Onna-son, Okinawa 904-0495, Japan myanagid@gmail.com.
authors.forename: Mitsuhiro
authors.initials: M
authors.lastname: Yanagida
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000595:Amino Acid Sequence; D020134:Catalytic Domain; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017124:Conserved Sequence; D004271:DNA, Fungal / Q000378:metabolism*; D004268:DNA-Binding Proteins; D008958:Models, Molecular; D046912:Multiprotein Complexes; D009154:Mutation; D010766:Phosphorylation; D017433:Protein Structure, Secondary; D012568:Schizosaccharomyces / Q000737:chemistry / Q000201:enzymology / Q000235:genetics*; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014638:Vanadates / Q000494:pharmacology
chemical_list: D002868:Chromosomal Proteins, Non-Histone; D004271:DNA, Fungal; D004268:DNA-Binding Proteins; D046912:Multiprotein Complexes; D029702:Schizosaccharomyces pombe Proteins; C108312:condensin complexes; D014638:Vanadates; D000251:Adenosine Triphosphatases
keywords: DNA re-annealing; auto-phosphorylation; condensin; hinge interface; hinge opening; mass spectrometry