On archaeal homologs of the human RNase P proteins Pop5 and Rpp30 in the hyperthermophilic archaeon Thermococcus kodakarensis

Kotaro Suematsu, Toshifumi Ueda, Takashi Nakashima, Yoshimitsu Kakuta, Makoto Kimura

研究成果: ジャーナルへの寄稿記事

3 引用 (Scopus)

抄録

The ribonuclease P (RNase P) proteins TkoPop5 and TkoRpp30, homologs of human Pop5 and Rpp30, respectively, in the hyperthermophilic archa-eon Thermococcus kodakarensis were prepared and characterized with respect to pre-tRNA cleavage activity using the reconstitution system of the well-studied Pyrococcus horikoshii RNase P. The reconstituted particle containing TkoPop5 in place of the P. horikoshii counterpart PhoPop5 retained pre-tRNA cleavage activity comparable to that of the reconstituted P. horikoshii RNase P, while that containing TkoRpp30 instead of its corresponding protein PhoRpp30 had slightly lower activity than the P. horikoshii RNase P. Moreover, we determined crystal structures of TkoRpp30 alone and in complex with TkoPop5. Like their P. horikoshii counterparts, whose structures were solved previously, TkoRpp30 and TkoPop5 fold into TIM barrel and RRM-like fold, respectively. This finding demonstrates that RNase P proteins in T. kodakarensis and P. horiko-shii are interchangeable and that their three-dimensional structures are highly conserved.

元の言語英語
ページ(範囲)952-959
ページ数8
ジャーナルBioscience, Biotechnology and Biochemistry
79
発行部数6
DOI
出版物ステータス出版済み - 1 1 2015

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Pyrococcus horikoshii
Thermococcus
Ribonuclease P
Archaea
RNA Precursors
Proteins
Crystal structure
human OCA2 protein

All Science Journal Classification (ASJC) codes

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

これを引用

On archaeal homologs of the human RNase P proteins Pop5 and Rpp30 in the hyperthermophilic archaeon Thermococcus kodakarensis. / Suematsu, Kotaro; Ueda, Toshifumi; Nakashima, Takashi; Kakuta, Yoshimitsu; Kimura, Makoto.

:: Bioscience, Biotechnology and Biochemistry, 巻 79, 番号 6, 01.01.2015, p. 952-959.

研究成果: ジャーナルへの寄稿記事

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abstract = "The ribonuclease P (RNase P) proteins TkoPop5 and TkoRpp30, homologs of human Pop5 and Rpp30, respectively, in the hyperthermophilic archa-eon Thermococcus kodakarensis were prepared and characterized with respect to pre-tRNA cleavage activity using the reconstitution system of the well-studied Pyrococcus horikoshii RNase P. The reconstituted particle containing TkoPop5 in place of the P. horikoshii counterpart PhoPop5 retained pre-tRNA cleavage activity comparable to that of the reconstituted P. horikoshii RNase P, while that containing TkoRpp30 instead of its corresponding protein PhoRpp30 had slightly lower activity than the P. horikoshii RNase P. Moreover, we determined crystal structures of TkoRpp30 alone and in complex with TkoPop5. Like their P. horikoshii counterparts, whose structures were solved previously, TkoRpp30 and TkoPop5 fold into TIM barrel and RRM-like fold, respectively. This finding demonstrates that RNase P proteins in T. kodakarensis and P. horiko-shii are interchangeable and that their three-dimensional structures are highly conserved.",
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AU - Ueda, Toshifumi

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AU - Kakuta, Yoshimitsu

AU - Kimura, Makoto

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