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

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)827-837
Number of pages11
JournalEMBO Journal
Volume17
Issue number3
DOIs
StatePublished - Feb 2 1998
Externally publishedYes

Fingerprint

Centromere Protein B
DNA
Centromere
Telomere-Binding Proteins
Mammalian Chromosomes
Nuclear magnetic resonance
human CENPB protein
Satellite DNA
Kinetochores
Amino Acid Sequence Homology
Chemical shift
Chromosomes
Yeast

Keywords

  • CENP-B
  • CENP-B box
  • Centromere
  • NMR structure
  • Protein-DNA interaction

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

Iwahara, J., Kigawa, T., Kitagawa, K., Masumoto, H., Okazaki, T., & Yokoyama, S. (1998). A helix-turn-helix structure unit in human centromere protein B (CENP-B). EMBO Journal, 17(3), 827-837. https://doi.org/10.1093/emboj/17.3.827

A helix-turn-helix structure unit in human centromere protein B (CENP-B). / Iwahara, Junji; Kigawa, Takanori; Kitagawa, Katsumi; Masumoto, Hiroshi; Okazaki, Tuneko; Yokoyama, Shigeyuki.

In: EMBO Journal, Vol. 17, No. 3, 02.02.1998, p. 827-837.

Research output: Contribution to journalArticle

Iwahara, J, Kigawa, T, Kitagawa, K, Masumoto, H, Okazaki, T & Yokoyama, S 1998, 'A helix-turn-helix structure unit in human centromere protein B (CENP-B)', EMBO Journal, vol. 17, no. 3, pp. 827-837. https://doi.org/10.1093/emboj/17.3.827
Iwahara J, Kigawa T, Kitagawa K, Masumoto H, Okazaki T, Yokoyama S. A helix-turn-helix structure unit in human centromere protein B (CENP-B). EMBO Journal. 1998 Feb 2;17(3):827-837. https://doi.org/10.1093/emboj/17.3.827
Iwahara, Junji ; Kigawa, Takanori ; Kitagawa, Katsumi ; Masumoto, Hiroshi ; Okazaki, Tuneko ; Yokoyama, Shigeyuki. / A helix-turn-helix structure unit in human centromere protein B (CENP-B). In: EMBO Journal. 1998 ; Vol. 17, No. 3. pp. 827-837.
@article{9d00fb4b9c834b558d001d61adc8e052,
title = "A helix-turn-helix structure unit in human centromere protein B (CENP-B)",
abstract = "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.",
keywords = "CENP-B, CENP-B box, Centromere, NMR structure, Protein-DNA interaction",
author = "Junji Iwahara and Takanori Kigawa and Katsumi Kitagawa and Hiroshi Masumoto and Tuneko Okazaki and Shigeyuki Yokoyama",
year = "1998",
month = "2",
day = "2",
doi = "10.1093/emboj/17.3.827",
language = "English (US)",
volume = "17",
pages = "827--837",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Nature Publishing Group",
number = "3",

}

TY - JOUR

T1 - A helix-turn-helix structure unit in human centromere protein B (CENP-B)

AU - Iwahara, Junji

AU - Kigawa, Takanori

AU - Kitagawa, Katsumi

AU - Masumoto, Hiroshi

AU - Okazaki, Tuneko

AU - Yokoyama, Shigeyuki

PY - 1998/2/2

Y1 - 1998/2/2

N2 - 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.

AB - 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.

KW - CENP-B

KW - CENP-B box

KW - Centromere

KW - NMR structure

KW - Protein-DNA interaction

UR - http://www.scopus.com/inward/record.url?scp=0032472955&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032472955&partnerID=8YFLogxK

U2 - 10.1093/emboj/17.3.827

DO - 10.1093/emboj/17.3.827

M3 - Article

VL - 17

SP - 827

EP - 837

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 3

ER -