Abstract:
:A defining feature of centromeres is the presence of the histone H3 variant CENP-A(Cnp1). It is not known how CENP-A(Cnp1) is specifically delivered to, and assembled into, centromeric chromatin. Through a screen for factors involved in kinetochore integrity in fission yeast, we identified Sim3. Sim3 is homologous to known histone binding proteins NASP(Human) and N1/N2(Xenopus) and aligns with Hif1(S. cerevisiae), defining the SHNi-TPR family. Sim3 is distributed throughout the nucleoplasm, yet it associates with CENP-A(Cnp1) and also binds H3. Cells defective in Sim3 function have reduced levels of CENP-A(Cnp1) at centromeres (and increased H3) and display chromosome segregation defects. Sim3 is required to allow newly synthesized CENP-A(Cnp1) to accumulate at centromeres in S and G2 phase-arrested cells in a replication-independent mechanism. We propose that one function of Sim3 is to act as an escort that hands off CENP-A(Cnp1) to chromatin assembly factors, allowing its incorporation into centromeric chromatin.
journal_name
Mol Celljournal_title
Molecular cellauthors
Dunleavy EM,Pidoux AL,Monet M,Bonilla C,Richardson W,Hamilton GL,Ekwall K,McLaughlin PJ,Allshire RCdoi
10.1016/j.molcel.2007.10.010subject
Has Abstractpub_date
2007-12-28 00:00:00pages
1029-44issue
6eissn
1097-2765issn
1097-4164pii
S1097-2765(07)00692-2journal_volume
28pub_type
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