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Recognition of centromere‐specific histone Cse4 by the inner kinetochore Okp1‐Ame1 complex

Journal Article · · EMBO Reports
 [1];  [2];  [1];  [3];  [4]
  1. Department of Biological Chemistry and Molecular Pharmacology Harvard Medical School, and Howard Hughes Medical Institute Boston MA USA
  2. Department of Bioengineering Jacobs School of Engineering, UCSD San Diego CA USA
  3. Department of Bioengineering Jacobs School of Engineering, UCSD San Diego CA USA, Department of Cellular and Molecular Medicine, School of Medicine Moores Cancer Center, UCSD San Diego CA USA
  4. Stanford Cancer Institute, Stanford School of Medicine Stanford CA USA
Abstract

Successful mitosis depends on the timely establishment of correct chromosomal attachments to microtubules. The kinetochore, a modular multiprotein complex, mediates this connection by recognizing specialized chromatin containing a histone H3 variant called Cse4 in budding yeast and CENP‐A in vertebrates. Structural features of the kinetochore that enable discrimination between Cse4/CENP‐A and H3 have been identified in several species. How and when these contribute to centromere recognition and how they relate to the overall structure of the inner kinetochore are unsettled questions. More generally, this molecular recognition ensures that only one kinetochore is built on each chromatid and that this happens at the right place on the chromatin fiber. We have determined the crystal structure of a Cse4 peptide bound to the essential inner kinetochore Okp1‐Ame1 heterodimer from budding yeast. The structure and related experiments show in detail an essential point of Cse4 contact and provide information about the arrangement of the inner kinetochore.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Organization:
National Institutes of Health (NIH); USDOE; USDOE Laboratory Directed Research and Development (LDRD) Program; USDOE National Nuclear Security Administration (NNSA)
Grant/Contract Number:
AC02-06CH11357
OSTI ID:
2217409
Alternate ID(s):
OSTI ID: 2470207
OSTI ID: 2217410
Journal Information:
EMBO Reports, Journal Name: EMBO Reports Journal Issue: 12 Vol. 24; ISSN 1469-221X
Publisher:
Nature Publishing GroupCopyright Statement
Country of Publication:
Germany
Language:
English

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