Biochemical analysis of the N-terminal domain of human RAD54B.

Naoyuki Sarai, Wataru Kagawa, Norie Fujikawa, Kengo Saito, Juri Hikiba, Kozo Tanaka, Kiyoshi Miyagawa, Hitoshi Kurumizaka, Shigeyuki Yokoyama

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The human RAD54B protein is a paralog of the RAD54 protein, which plays important roles in homologous recombination. RAD54B contains an N-terminal region outside the SWI2/SNF2 domain that shares less conservation with the corresponding region in RAD54. The biochemical roles of this region of RAD54B are not known, although the corresponding region in RAD54 is known to physically interact with RAD51. In the present study, we have biochemically characterized an N-terminal fragment of RAD54B, consisting of amino acid residues 26-225 (RAD54B(26-225)). This fragment formed a stable dimer in solution and bound to branched DNA structures. RAD54B(26-225) also interacted with DMC1 in both the presence and absence of DNA. Ten DMC1 segments spanning the entire region of the DMC1 sequence were prepared, and two segments, containing amino acid residues 153-214 and 296-340, were found to directly bind to the N-terminal domain of RAD54B. A structural alignment of DMC1 with the Methanococcus voltae RadA protein, a homolog of DMC1 in the helical filament form, indicated that these RAD54B-binding sites are located near the ATP-binding site at the monomer-monomer interface in the DMC1 helical filament. Thus, RAD54B binding may affect the quaternary structure of DMC1. These observations suggest that the N-terminal domain of RAD54B plays multiple roles of in homologous recombination.

Original languageEnglish
Pages (from-to)5441-5450
Number of pages10
JournalNucleic Acids Research
Volume36
Issue number17
DOIs
Publication statusPublished - 2008 Oct
Externally publishedYes

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Homologous Recombination
Amino Acids
Methanococcus
Binding Sites
DNA
Proteins
Adenosine Triphosphate
human RAD54B protein

ASJC Scopus subject areas

  • Genetics

Cite this

Sarai, N., Kagawa, W., Fujikawa, N., Saito, K., Hikiba, J., Tanaka, K., ... Yokoyama, S. (2008). Biochemical analysis of the N-terminal domain of human RAD54B. Nucleic Acids Research, 36(17), 5441-5450. https://doi.org/10.1093/nar/gkn516

Biochemical analysis of the N-terminal domain of human RAD54B. / Sarai, Naoyuki; Kagawa, Wataru; Fujikawa, Norie; Saito, Kengo; Hikiba, Juri; Tanaka, Kozo; Miyagawa, Kiyoshi; Kurumizaka, Hitoshi; Yokoyama, Shigeyuki.

In: Nucleic Acids Research, Vol. 36, No. 17, 10.2008, p. 5441-5450.

Research output: Contribution to journalArticle

Sarai, N, Kagawa, W, Fujikawa, N, Saito, K, Hikiba, J, Tanaka, K, Miyagawa, K, Kurumizaka, H & Yokoyama, S 2008, 'Biochemical analysis of the N-terminal domain of human RAD54B.', Nucleic Acids Research, vol. 36, no. 17, pp. 5441-5450. https://doi.org/10.1093/nar/gkn516
Sarai N, Kagawa W, Fujikawa N, Saito K, Hikiba J, Tanaka K et al. Biochemical analysis of the N-terminal domain of human RAD54B. Nucleic Acids Research. 2008 Oct;36(17):5441-5450. https://doi.org/10.1093/nar/gkn516
Sarai, Naoyuki ; Kagawa, Wataru ; Fujikawa, Norie ; Saito, Kengo ; Hikiba, Juri ; Tanaka, Kozo ; Miyagawa, Kiyoshi ; Kurumizaka, Hitoshi ; Yokoyama, Shigeyuki. / Biochemical analysis of the N-terminal domain of human RAD54B. In: Nucleic Acids Research. 2008 ; Vol. 36, No. 17. pp. 5441-5450.
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