2000
DOI: 10.1126/science.288.5474.2215
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Requirement of Mis6 Centromere Connector for Localizing a CENP-A-Like Protein in Fission Yeast

Abstract: Mammalian kinetochores contain the centromere-specific histone H3 variant CENP-A, whose incorporation into limited chromosomal regions may be important for centromere function and chromosome segregation during mitosis. However, regulation of CENP-A localization and its role have not been clear. Here we report that the fission yeast homolog SpCENP-A is essential for establishing centromere chromatin associated with equal chromosome segregation. SpCENP-A binding to the nonrepetitious inner centromeres depended o… Show more

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Cited by 368 publications
(467 citation statements)
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“…In S. cerevisiae, centromere localization of meiotic cohesin Rec8 is reduced by loss of CHL4 (Marston et al, 2004), which is a homolog of S. pombe Mis15, and Mis15 requires Mis6 for its centromere localization (Hayashi et al, 2004). Mis6 is also required for loading of Cnp1, a CENP-A homolog (Takahashi et al, 2000). Thus, the Mis6 complex forms a "foothold" for the Rec8-mediated mono-orientation kinetochore, most likely through interactions with CENP-Aand CENP-C-associated regions of the centromere ( Figure 10A).…”
Section: Mis6 Complex: Basic Architecture Of the Kinetochorementioning
confidence: 99%
See 1 more Smart Citation
“…In S. cerevisiae, centromere localization of meiotic cohesin Rec8 is reduced by loss of CHL4 (Marston et al, 2004), which is a homolog of S. pombe Mis15, and Mis15 requires Mis6 for its centromere localization (Hayashi et al, 2004). Mis6 is also required for loading of Cnp1, a CENP-A homolog (Takahashi et al, 2000). Thus, the Mis6 complex forms a "foothold" for the Rec8-mediated mono-orientation kinetochore, most likely through interactions with CENP-Aand CENP-C-associated regions of the centromere ( Figure 10A).…”
Section: Mis6 Complex: Basic Architecture Of the Kinetochorementioning
confidence: 99%
“…Recently 13 proteins were purified as a Mis6-containing complex by biochemical purification . These proteins include Sim4 and Mis15, which have been reported to depend on the Mis6 protein for their centromere localization (Takahashi et al, 2000;Pidoux et al, 2003;Hayashi et al, 2004). Thus, it is likely that these proteins compose the Mis6 complex (also called the Sim4 complex in Liu et al, 2005), which corresponds to the S. cerevisiae COMA and Ctf19 complexes.…”
Section: Introductionmentioning
confidence: 99%
“…One hallmark of all kinetochores is the essential CenH3 (Palmer et al, 1987;Stoler et al, 1995;Buchwitz et al, 1999;Henikoff et al, 2000;Takahashi et al, 2000;Sanyal and Carbon, 2002;Talbert et al, 2002;Zhong et al, 2002;Edwards and Murray, 2005). CenH3s contain a unique N terminus and a well-conserved C terminus that is highly homologous to histone H3 (Malik and Henikoff, 2003).…”
Section: Introductionmentioning
confidence: 99%
“…Outer kinetochore complexes include the conserved NDC80 (Ndc80, Spc24, Spc25, and Nuf2) and DAM1 (Dam1, Ask1, Duo1, Dad1, Dad2, Dad3, Dad4, Spc19, Spc34, and Hsk3) complexes. DAM1 is considered to be the outermost complex because it requires microtubules and all other complexes for kinetochore localization (Enquist-Newman et al, 2001;Janke et al, 2002;Li et al, 2002).One hallmark of all kinetochores is the essential CenH3 (Palmer et al, 1987;Stoler et al, 1995;Buchwitz et al, 1999;Henikoff et al, 2000;Takahashi et al, 2000;Sanyal and Carbon, 2002;Talbert et al, 2002;Zhong et al, 2002;Edwards and Murray, 2005). CenH3s contain a unique N terminus and a well-conserved C terminus that is highly homologous to histone H3 (Malik and Henikoff, 2003).…”
mentioning
confidence: 99%
“…This indicates that functional CENP-A nucleosomes are assembled into chromatin as a consequence of CENP-C or CENP-I ectopic localization . Indeed, the individual CENPs that comprise the recently identified CENP-H/I/K/M complex have been implicated in CENP-A assembly in chicken and human cells (Takahashi et al 2000;Okada et al 2006).…”
Section: The Centromerementioning
confidence: 99%