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

Research output: Contribution to journalArticle

16 Citations (Scopus)

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-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.

Original languageEnglish
Pages (from-to)749-758
Number of pages10
JournalBioscience, Biotechnology and Biochemistry
Volume72
Issue number3
DOIs
Publication statusPublished - 2008

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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