A distinct binding mode of archaeal ribonuclease P proteins to RNA

Masato Ishihara; Etsuko Nishimoto; Shoji Yamashita; Yoshimitsu Kakuta; Makoto Kimura

doi:10.1271/bbb.120546

A distinct binding mode of archaeal ribonuclease P proteins to RNA

Masato Ishihara, Etsuko Nishimoto, Shoji Yamashita, Yoshimitsu Kakuta, Makoto Kimura

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

The ribonuclease P (RNase P) in the hyperthermophilic archaeon Pyrococcus horikoshii comprises RNA (PhopRNA) and five proteins. We analyzed the RNA binding mode of the protein, using a pair of complementary fluorescence-labeled oligoribonucleotides. Fluorescence resonance energy transfer (FRET)-based assays suggested that the RNase P proteins assist PhopRNA in attaining a functionally active conformation via a distinct mode of binding.

Original language	English
Pages (from-to)	2335-2337
Number of pages	3
Journal	Bioscience, Biotechnology and Biochemistry
Volume	76
Issue number	12
DOIs	https://doi.org/10.1271/bbb.120546
Publication status	Published - 2012

All Science Journal Classification (ASJC) codes

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

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abstract = "The ribonuclease P (RNase P) in the hyperthermophilic archaeon Pyrococcus horikoshii comprises RNA (PhopRNA) and five proteins. We analyzed the RNA binding mode of the protein, using a pair of complementary fluorescence-labeled oligoribonucleotides. Fluorescence resonance energy transfer (FRET)-based assays suggested that the RNase P proteins assist PhopRNA in attaining a functionally active conformation via a distinct mode of binding.",

author = "Masato Ishihara and Etsuko Nishimoto and Shoji Yamashita and Yoshimitsu Kakuta and Makoto Kimura",

note = "Funding Information: This work was supported by a grant-in-aid for scientific research from the Ministry of Education, Culture, Sports, Science, and Technology of Japan (to M.K., no. 22380062).",

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doi = "10.1271/bbb.120546",

language = "English",

volume = "76",

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T1 - A distinct binding mode of archaeal ribonuclease P proteins to RNA

AU - Ishihara, Masato

AU - Nishimoto, Etsuko

AU - Yamashita, Shoji

AU - Kakuta, Yoshimitsu

AU - Kimura, Makoto

N1 - Funding Information: This work was supported by a grant-in-aid for scientific research from the Ministry of Education, Culture, Sports, Science, and Technology of Japan (to M.K., no. 22380062).

PY - 2012

Y1 - 2012

N2 - The ribonuclease P (RNase P) in the hyperthermophilic archaeon Pyrococcus horikoshii comprises RNA (PhopRNA) and five proteins. We analyzed the RNA binding mode of the protein, using a pair of complementary fluorescence-labeled oligoribonucleotides. Fluorescence resonance energy transfer (FRET)-based assays suggested that the RNase P proteins assist PhopRNA in attaining a functionally active conformation via a distinct mode of binding.

AB - The ribonuclease P (RNase P) in the hyperthermophilic archaeon Pyrococcus horikoshii comprises RNA (PhopRNA) and five proteins. We analyzed the RNA binding mode of the protein, using a pair of complementary fluorescence-labeled oligoribonucleotides. Fluorescence resonance energy transfer (FRET)-based assays suggested that the RNase P proteins assist PhopRNA in attaining a functionally active conformation via a distinct mode of binding.

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JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 12

ER -

A distinct binding mode of archaeal ribonuclease P proteins to RNA

Abstract

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