Crystal Structure and Functional Analysis of an Archaeal Chromatin Protein Alba from the Hyperthermophilic Archaeon Pyrococcus horikoshii OT3

Kazumasa HADA; Takashi NAKASHIMA; Takuo OSAWA; Hiroaki SHIMADA; Yoshimitsu KAKUTA; Makoto KIMURA

doi:10.1271/bbb.70639

Biochemistry & Molecular Biology Regular Papers

Crystal Structure and Functional Analysis of an Archaeal Chromatin Protein Alba from the Hyperthermophilic Archaeon Pyrococcus horikoshii OT3

Kazumasa HADA, Takashi NAKASHIMA, Takuo OSAWA, Hiroaki SHIMADA, Yoshimitsu KAKUTA, Makoto KIMURA

Author information

Kazumasa HADA
Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University
Takashi NAKASHIMA
Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University
Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University
Takuo OSAWA
Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University
Hiroaki SHIMADA
Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University
Yoshimitsu KAKUTA
Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University
Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University
Makoto KIMURA
Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University
Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University

Keywords: Alba, crystal structure, precursor tRNA (pre-tRNA), Pyrococcus horikoshii, ribonuclease P (RNase P)

JOURNAL FREE ACCESS

2008 Volume 72 Issue 3 Pages 749-758

DOI https://doi.org/10.1271/bbb.70639

View "Advance Publication" version (March 7, 2008).

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Abstract

The crystal structure of the Alba protein (PhoAlba) from a hyperthermophilic archaeon, Pyrococcus horikoshii OT3, was determined at a resolution of 2.8 Å. PhoAlba structurally belongs to the α⁄β proteins and is similar not only to archaeal homologues but also to RNA-binding proteins, including the C-terminal half of initiation factor 3 (IF3-C) from Bacillus stearothermophilus, an Esherichia coli protein implicated in cell division (Yhhp), and an Arabidopsis protein of unknown function. We found by gel shift assay that PhoAlba interacts with both ribonuclease P (RNase P) RNA (PhopRNA) and precursor-tRNA^Tyr (pre-tRNA^Tyr) in P. horikoshii. However, the addition of PhoAlba to reconstituted particles composed of PhopRNA and four or five protein subunits had little influence on either the pre-tRNA processing activity or the optimum temperature for the processing activity. These results suggest that PhoAlba contributes little to the catalytic activity of P. horikoshii RNase P.

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