Recognition of the centromere-binding protein Ndc10 by Scm3HJURP directs Cse4CENP-A deposition at native centromeres

Scm3HJURP recognition of Ndc10 directs centromere-specific Cse4CENP-A deposition at native centromeres, with Scm3–Cse4–H4 complexes strongly boosting assembly in yeast cell-free extracts.

• Why it matters: Native centromeres assemble CENP-A inefficiently in cell-free systems, implying limiting factors that determine where Cse4CENP-A is deposited.
• What they did: In Saccharomyces cerevisiae extracts, adding Scm3–Cse4–histone H4 stimulates Cse4 assembly in a centromeric DNA sequence- and dose-dependent manner, with stronger improvements in mitotic than interphase (G1) extracts.
• The result: In a complemented cell-free reconstitution, distinct Scm3 interfaces with Cse4 and with Ndc10 are essential for centromere-specific Cse4 assembly and cell viability, implying locus-specific deposition is Ndc10-directed.

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