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

研究成果: ジャーナルへの寄稿記事

15 引用 (Scopus)

抄録

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.

元の言語英語
ページ(範囲)749-758
ページ数10
ジャーナルBioscience, Biotechnology and Biochemistry
72
発行部数3
DOI
出版物ステータス出版済み - 4 7 2008

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Pyrococcus horikoshii
Archaeal Proteins
Functional analysis
Archaea
Ribonuclease P
Chromatin
Crystal structure
RNA Precursors
RNA, Transfer, Tyr
Arabidopsis Proteins
Geobacillus stearothermophilus
Peptide Initiation Factors
Proteins
RNA-Binding Proteins
Protein Subunits
Bacilli
Processing
Protein C
Cell Division
Assays

All Science Journal Classification (ASJC) codes

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

これを引用

Crystal structure and functional analysis of an archaeal chromatin protein alba from the hyperthermophilic archaeon Pyrococcus horikoshii OT3. / Hada, Kazumasa; Nakashima, Takashi; Osawa, Takuo; Shimada, Hiroaki; Kakuta, Yoshimitsu; Kimura, Makoto.

:: Bioscience, Biotechnology and Biochemistry, 巻 72, 番号 3, 07.04.2008, p. 749-758.

研究成果: ジャーナルへの寄稿記事

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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 {\AA}. 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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AU - Hada, Kazumasa

AU - Nakashima, Takashi

AU - Osawa, Takuo

AU - Shimada, Hiroaki

AU - Kakuta, Yoshimitsu

AU - Kimura, Makoto

PY - 2008/4/7

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N2 - 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.

AB - 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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