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PDBsum entry 4xyh
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References listed in PDB file
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Key reference
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Title
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Mis16 independently recognizes histone h4 and the cenp-Acnp1-Specific chaperone scm3sp.
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Authors
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S.An,
H.Kim,
U.S.Cho.
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Ref.
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J Mol Biol, 2015,
427,
3230-3240.
[DOI no: ]
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PubMed id
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Abstract
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CENP-A is a centromere-specific histone H3 variant that is required for
kinetochore assembly and accurate chromosome segregation. For it to function
properly, CENP-A must be specifically localized to centromeres. In fission
yeast, Scm3sp and the Mis18 complex, composed of Mis16, Eic1, and Mis18,
function as a CENP-A(Cnp1)-specific chaperone and a recruiting factor,
respectively, and together ensure accurate delivery of CENP-A(Cnp1) to
centromeres. Although how Scm3sp specifically recognizes CENP-A(Cnp1) has been
revealed recently, the recruiting mechanism of CENP-A(Cnp1) via the Mis18
complex remains unknown. In this study, we have determined crystal structures of
Schizosaccharomyces japonicus Mis16 alone and in complex with the helix 1 of
histone H4 (H4α1). Crystal structures followed by mutant analysis and affinity
pull-downs have revealed that Mis16 recognizes both H4α1 and Scm3sp
independently within the CENP-A(Cnp1)/H4:Scm3sp complex. This observation
suggests that Mis16 gains CENP-A(Cnp1) specificity by recognizing both Scm3sp
and histone H4. Our studies provide insights into the molecular mechanisms
underlying specific recruitment of CENP-A(Cnp1)/H4:Scm3sp into centromeres.
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