Chromosome dynamics: the SMC protein family

Jessberger, Rolf; Frei, C.; Gasser, Susan M.

doi:10.1016/s0959-437x(98)80149-4

Cited by 76 publications

(69 citation statements)

References 31 publications

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“…Of interest is that yeast centromere DNA, a prominent cohesion site that is A/T rich and contains inverted palindromic repeats, is one of many efficient competitors of Smc1p substrate binding (Akhmedov et al 1998(Akhmedov et al ,1999. Eukaryotic SMCs most likely assemble into heterodimers (Hirano 1998;Jessberger et al 1998;Nasmyth 1999). Note that bacterial SMC proteins are singly represented in the genome and thus assemble into homodimers (Melby et al 1998).…”

Section: Establishing Cohesionmentioning

confidence: 99%

Holding Your Own: Establishing Sister Chromatid Cohesion

Skibbens

2000

Genome Research

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Section: Establishing Cohesionmentioning

confidence: 99%

Holding Your Own: Establishing Sister Chromatid Cohesion

Skibbens

2000

Genome Research

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“…Proteins belonging to the Smc family also exist in bacteria, which suggests that Smc proteins are modulators of chromosome structure that must have existed in the common ancestor of all living organisms. Members of the Smc protein family have been implicated in chromosome condensation, dosage compensation, and in DNA 1 repair (Jessberger et al 1998). Two pieces of evidence suggest that Scc1p binds to chromosomes as part of a Cohesin complex with Smc1p and Smc3p.…”

mentioning

confidence: 99%

Yeast Cohesin complex requires a conserved protein, Eco1p(Ctf7), to establish cohesion between sister chromatids during DNA replication

Tóth¹,

Ciosk²,

Uhlmann³

et al. 1999

Genes & Development

579

679

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Sister chromatid cohesion is crucial for chromosome segregation during mitosis. Loss of cohesion very possibly triggers sister separation at the metaphase → anaphase transition. This process depends on the destruction of anaphase inhibitory proteins like Pds1p (Cut2p), which is thought to liberate a sister-separating protein Esp1p (Cut1p). By looking for mutants that separate sister centromeres in the presence of Pds1p, this and a previous study have identified six proteins essential for establishing or maintaining sister chromatid cohesion. Four of these proteins, Scc1p, Scc3p, Smc1p, and Smc3p, are subunits of a 'Cohesin' complex that binds chromosomes from late G 1 until the onset of anaphase. The fifth protein, Scc2p, is not a stoichiometric Cohesin subunit but it is required for Cohesin's association with chromosomes. The sixth protein, Eco1p(Ctf7p), is not a Cohesin subunit. It is necessary for the establishment of cohesion during DNA replication but not for its maintenance during G 2 and M phases.

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“…DNA topoisomerase II (topo II) and subtypes of SMC (structural maintenance of chromosomes; Strunnikov et al 1995) proteins are known to be required for condensation (Uemura et al 1987;Adachi et al 1991;Hirano andMitchison 1993,1994;Saka et al 1994;Strunnikov et al 1995; for review, see Saitoh et al 1995). The SMC proteins are highly conserved in evolution (Hirano 1998;Jessberger et al 1998;Strunnikov 1998), with frog XCAP-E, budding yeast Smc2p, and fission yeast Cut14 constituting one subtype, and XCAP-C, Smc4p, and Cut3 forming another subtype. Condensin complex containing SMC2 and SMC4 was first identified in frog cell extracts as a five-member complex and shown to be essential for an in vitro reconstitution system of mitotic chromosome condensation (Hirano and Mitchison 1994;Hirano et al 1997).…”

mentioning

confidence: 99%

Fission yeast condensin complex: essential roles of non-SMC subunits for condensation and Cdc2 phosphorylation of Cut3/SMC4

Sutani¹,

Yuasa²,

Tomonaga³

et al. 1999

Genes & Development

246

280

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The condensin complex in frog extracts, containing two SMC (structural maintenance of chromosomes) and three non-SMC subunits, promotes mitotic chromosome condensation, and its supercoiling activity increases during mitosis by Cdc2 phosphorylation. Here, we report that fission yeast has the same five-member condensin complex, each of which is essential for mitotic condensation. The condensin complex was purified and the subunits were identified by microsequencing. Cnd1, Cnd2, and Cnd3, three non-SMC subunits showing a high degree of sequence conservation to frog subunits, are essential for viability, and their gene disruption leads to a phenotype indistinguishable from that observed in cut3-477 and cut14-208, known mutations in SMC4 and SMC2-like subunits. Condensin subunits tagged with GFP were observed to alter dramatically their localization during the cell cycle, enriched in the nucleus during mitosis, but cytoplasmic during other stages. This stage-specific alteration in localization requires mitosis-specific phosphorylation of the T19 Cdc2 site in Cut3. The T19 site is phosphorylated in vitro by Cdc2 kinase and shows the maximal phosphorylation in metaphase in vivo. Its alanine substitution mutant fails to suppress the temperature-sensitive phenotype of cut3-477, and shows deficiency in condensation, probably because Cut3 T19A remains cytoplasmic. Therefore, direct Cdc2 phosphorylation of fission yeast condensin may facilitate its nuclear accumulation during mitosis.

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Chromosome dynamics: the SMC protein family

Cited by 76 publications

References 31 publications

Holding Your Own: Establishing Sister Chromatid Cohesion

Holding Your Own: Establishing Sister Chromatid Cohesion

Yeast Cohesin complex requires a conserved protein, Eco1p(Ctf7), to establish cohesion between sister chromatids during DNA replication

Fission yeast condensin complex: essential roles of non-SMC subunits for condensation and Cdc2 phosphorylation of Cut3/SMC4

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