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

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概要

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• 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-tRNATyr (pre-tRNATyr) 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.

• 社団法人 日本農芸化学会の論文

著者

• KIMURA Makoto

  Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University

• Hada Kazumasa

  Laboratory Of Biochemistry Department Of Bioscience And Biotechnology Faculty Of Agriculture Graduat

• Nakashima Takashi

  Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University

• Osawa Takuo

  Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University

• SHIMADA Hiroaki

  Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University

• KAKUTA Yoshimitsu

  Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Kyushu University

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