Identification of a novel zinc-binding protein, C1orf123, as an interactor with a heavy metalassociated domain

Yoshiaki Furukawa, Carolyn Lim, Takehiko Tosha, Koki Yoshida, Tomoaki Hagai, Shuji Akiyama, Shoji Watanabe, Kenta Nakagome, Yoshitsugu Shiro

研究成果: Article査読

5 被引用数 (Scopus)

抄録

Heavy metal-associated (HMA) domains bind metal ions at its Cys-x-x-Cys (CxxC) motif and constitute an intracellular network for trafficking of metal ions for utilization and detoxification. We thus expect that novel metalloproteins can be identified by screening proteins interacting with a HMA domain. In this study, we performed yeast two-hybrid screening of the human proteome and found an uncharacterized protein encoded as open reading frame 123 in chromosome 1 (C1orf123) that can interact specifically with the HMA domain of a copper chaperone for superoxide dismutase (CCSdI). Our X-ray structural analysis of C1orf123 further revealed that it binds a Zn 2+ ion in a tetrahedral coordination with four thiolate groups from two conserved CxxC motifs. For the interaction between C1orf123 and CCSdI, the CxxC motifs in both C1orf123 and CCSdI were required, implying metal-mediated interaction through the CxxC motifs. Notably, C1orf123 did not interact with several other HMA domains containing CxxC motifs, supporting high specificity in the interaction between C1orf123 and CCSdI. Based upon these results, we further discuss functional and structural significance of the interaction between C1orf123 and CCS.

本文言語English
論文番号e0204355
ジャーナルPloS one
13
9
DOI
出版ステータスPublished - 2018 9月

ASJC Scopus subject areas

  • 生化学、遺伝学、分子生物学(全般)
  • 農業および生物科学(全般)
  • 一般

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