In vivo functional dissection of human inner kinetochore protein CENP-C

CENP-C is a fundamental component of the inner kinetochore plate and contributes to the formation of functional centromeres in eukaryotic organisms. Recruitment of CENP-C to kinetochore requires other centromere proteins, particularly CENP-A, CENP-H, and CENP-I. However, how CENP-C is correctly loca...

Full description

Saved in:
Bibliographic Details
Published in:Journal of structural biology 2002-10, Vol.140 (1), p.39-48
Main Authors: Trazzi, Stefania, Bernardoni, Roberto, Diolaiti, Daniel, Politi, Valeria, Earnshaw, William C., Perini, Giovanni, Della Valle, Giuliano
Format: Article
Language:English
Subjects:
Blotting, Western
CENP-C
Centromere - chemistry
Centromere localization domain
Chromatin - metabolism
Chromosomal Proteins, Non-Histone - chemistry
Chromosomal Proteins, Non-Histone - genetics
Chromosomal Proteins, Non-Histone - physiology
Cross-Linking Reagents - pharmacology
DNA binding domain
DNA, Satellite - metabolism
Electrophoresis, Polyacrylamide Gel
Formaldehyde - pharmacology
Humans
Kinetochore
Kinetochores - metabolism
Microscopy, Fluorescence
Mutation
Precipitin Tests
Protein Structure, Tertiary
α-Satellite DNA
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:CENP-C is a fundamental component of the inner kinetochore plate and contributes to the formation of functional centromeres in eukaryotic organisms. Recruitment of CENP-C to kinetochore requires other centromere proteins, particularly CENP-A, CENP-H, and CENP-I. However, how CENP-C is correctly localized at the kinetochore is not clearly determined, mainly due to the functional variety of its domains, which hints at a complex recruitment mechanism. Here, by both immunofluorescent labeling and chromatin/immunoprecipitation we could show that human CENP-C contains two distinct domains, one in the central region, between amino acids 426 and 537, and the second one in the carboxyl terminal region, between amino acids 638 and 943, which are both capable of localizing at centromeres and binding α-satellite DNA. The presence of two domains that iterate the same function despite being significantly different in their amino acid sequence and structure suggests that CENP-C may target the centromere by establishing multiple contacts with both the DNA and protein constituents of the kinetochore.
ISSN:1047-8477
1095-8657
DOI:10.1016/S1047-8477(02)00506-3