A helix-turn-helix structure unit in human centromere protein B (CENP-B)

Junji Iwahara, Takanori Kigawa, Katsumi Kitagawa, Hiroshi Masumoto, Tuneko Okazaki, Shigeyuki Yokoyama

Producción científica: Articlerevisión exhaustiva

34 Citas (Scopus)

Resumen

CENP-B has been suggested to organize arrays of centromere satellite DNA into a higher order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes. The N-terminal portion of CENP-B is a 15 kDa DNA binding domain (DBD) consisting of two repeating units, RP1 and RP2. The DBD specifically binds to the CENP-B box sequence (17 bp) in centromere DNA. We determined the solution structure of human CENP-B DBD RP1 by multi-dimensional 1H, 13C and 15N NMR methods. The CENP-B DBD RP1 structure consists of four helices and has a helix-turn-helix structure. The overall folding is similar to those of some other eukaryotic DBDs, although significant sequence homology with these proteins was not found. The DBD of yeast RAP1, a telomere binding protein, is most similar to CENP-B DBD RP1. We studied the interaction between CENP-B DBD RP1 and the CENP-B box by the use of NMR chemical shift perturbation. The results suggest that CENP-B DBD RP1 interacts with one of the essential regions of the CENP-B box DNA, mainly at the N-terminal basic region, the N-terminal portion of helix 2 and helix 3.

Idioma originalEnglish (US)
Páginas (desde-hasta)827-837
Número de páginas11
PublicaciónEMBO Journal
Volumen17
N.º3
DOI
EstadoPublished - feb 2 1998
Publicado de forma externa

ASJC Scopus subject areas

  • General Immunology and Microbiology
  • General Biochemistry, Genetics and Molecular Biology
  • Molecular Biology
  • General Neuroscience

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