Fission Yeast Scm3: A CENP-A Receptor Required for Integrity of Subkinetochore Chromatin

Pidoux, Alison L.; Choi, Eui Sung; Abbott, Johanna; Liu, Xingkun; Kagansky, Alexander; Castillo, Araceli G.; Hamilton, Georgina L.; Richardson, W A R; Rappsilber, Juri; He, Xiangwei; Allshire, Robin C.

doi:10.1016/j.molcel.2009.01.019

Cited by 182 publications

(297 citation statements)

References 55 publications

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“…23,24 Fission yeast Cnp1 and mammalian CENP-A are stably assembled into centromeres in S/G 2 phase and early G 1 , respectively, thus outside DNA replication when canonical nucleosomes are incorporated into chromatin. 20,23,25 Consistent with this, Sp Scm3 binds to centromeres in mid-late anaphase and dissociates with spindle formation in early mitosis. 20 Localization of HJURP at centromeres is also cell cycle regulated.…”

Section: Introductionsupporting

confidence: 66%

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The CENP-A chaperone Scm3 becomes enriched at kinetochores in anaphase independently of CENP-A incorporation

et al. 2011

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Section: Introductionsupporting

confidence: 66%

“…18,19 In S. pombe, Sp Scm3 targets Cnp1 to centromeres through binding to the proteins Mis16 and Mis18. 20,21 Bioinformatical evidences suggest that HJURP is the human homolog of Scm3. cells and finally immunoprecipitated Scm3-TAP bound to DNA with IgG dynabeads.…”

Section: Introductionmentioning

confidence: 99%

The CENP-A chaperone Scm3 becomes enriched at kinetochores in anaphase independently of CENP-A incorporation

et al. 2011

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“…Interestingly, Mc was found to be enriched at the promoter region of scm3 (Fig. 3B), which encodes a chaperone involved in loading of the centromere-specific histone H3 variant, CENP-A (36)(37)(38). Mc likely induces the expression of this locus because a previous study has shown that scm3 is expressed at higher levels in M cells, compared with P cells (35).…”

Section: Resultsmentioning

confidence: 90%

A homolog of male sex-determining factor SRY cooperates with a transposon-derived CENP-B protein to control sex-specific directed recombination

Matsuda

Sugioka-Sugiyama

Mizuguchi

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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Schizosaccharomyces pombe cells switch mating type by replacing genetic information at the expressed mat1 locus with sequences copied from mat2-P or mat3-M silent donor loci. The choice of donor locus is dictated by cell type, such that mat2 is the preferred donor in M cells and mat3 is the preferred donor in P cells. Donor choice involves a recombination-promoting complex (RPC) containing Swi2 and Swi5. In P cells, the RPC localizes to a specific DNA element located adjacent to mat3, but in M cells it spreads across the silent mating-type region, including mat2-P. This differential distribution of the RPC regulates nonrandom choice of donors. However, celltype-specific differences in RPC localization are not understood. Here we show that the mat1-M-encoded factor Mc, which shares structural and functional similarities with the male sex-determining factor SRY, is highly enriched at the swi2 and swi5 loci and promotes elevated levels of RPC components. Loss of Mc reduces Swi2 and Swi5 to levels comparable to those in P cells and disrupts RPC spreading across the mat2/3 region. Mc also localizes to loci expressed preferentially in M cells and to retrotransposon LTRs. We demonstrate that Mc localization at LTRs and at swi2 requires Abp1, a homolog of transposon-derived CENP-B protein and that loss of Abp1 impairs Swi2 protein expression and the donor choice mechanism. These results suggest that Mc modulates levels of recombination factors, which is important for mating-type donor selection and for the biased gene conversion observed during meiosis, where M cells serve as preferential donors of genetic information. (1) and mating-type switching in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe (2-5). In these distantly related yeast species, cells alternate between two distinct mating-type alleles by copying genetic information from one of the two silent donor loci to the active mating-type locus via highly orchestrated recombination processes (6-8).The mating-type region of S. pombe contains three linked locimat1, mat2, and mat3-located on chromosome 2. In wild-type homothallic strains, designated h 90 , mat2 is located ∼17 kb centromere-distal to mat1, whereas mat3 is separated from mat2 by an 11-kb interval ( Fig. 1) (8, 9). The mating type of a haploid cell is determined by the presence of P or M information at mat1 (8). Each allele consists of two divergently transcribed genes (10). mat1-P contains the Pc and Pi genes, and mat1-M contains the Mc and Mi genes. mat2 and mat3 contain the same genetic information as mat1-P and mat1-M, respectively, but are maintained in a silent state. These silent mating-type cassettes are embedded in a 20-kb heterochromatin domain surrounded by inverted repeat (IR-R and IR-

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“…The human proteins hMis18 and M18BP1, recruited to centromere at telophase-G1, and RbAp46/RbAp48 may act to prime centromere for CENP-A localization (21). In S. cerivisiae and S. pombe, Scm3 (Suppressor of chromosome mis-segregation 3) protein was shown to specifically bind the CenH3-H4 complex and to be required for its assembly into the centromeric chromatin (22)(23)(24)(25)(26).…”

mentioning

confidence: 99%

HJURP binds CENP-A via a highly conserved N-terminal domain and mediates its deposition at centromeres

Shuaib

Ouararhni

Dimitrov

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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193

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The human histone H3 variant, CENP-A, replaces the conventional histone H3 in centromeric chromatin and, together with centromerespecific DNA-binding factors, directs the assembly of the kinetochore. We purified the prenucelosomal e-CENP-A complex. We found that HJURP, a member of the complex, was required for cell cycle specific targeting of CENP-A to centromeres. HJURP facilitated efficient deposition of CENP-A/H4 tetramers to naked DNA in vitro. Bacterially expressed HJURP binds at a stoichiometric ratio to the CENP-A/H4 tetramer but not to the H3/H4 tetramer. The binding occurred through a conserved HJURP short N-terminal domain, termed CBD. The novel characteristic identified in vertebrates that we named TLTY box of CBD, was essential for formation of the HJURP-CENP-A/H4 complex. Our data identified HJURP as a vertebrate CENP-A chaperone and dissected its mode of interactions with CENP-A.histone chaperone | histone variant

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Fission Yeast Scm3: A CENP-A Receptor Required for Integrity of Subkinetochore Chromatin

Cited by 182 publications

References 55 publications

The CENP-A chaperone Scm3 becomes enriched at kinetochores in anaphase independently of CENP-A incorporation

The CENP-A chaperone Scm3 becomes enriched at kinetochores in anaphase independently of CENP-A incorporation

A homolog of male sex-determining factor SRY cooperates with a transposon-derived CENP-B protein to control sex-specific directed recombination

HJURP binds CENP-A via a highly conserved N-terminal domain and mediates its deposition at centromeres

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