Thermodynamic analysis of a multifunctional RNA-binding protein, PhoRpp38, in the hyperthermophilic archaeon Pyrococcus horikoshii OT3

Kosuke Oshima; Takashi Nakashima; Yoshimitsu Kakuta; Kouhei Tsumoto; Makoto Kimura

doi:10.1271/bbb.120272

Thermodynamic analysis of a multifunctional RNA-binding protein, PhoRpp38, in the hyperthermophilic archaeon Pyrococcus horikoshii OT3

Kosuke Oshima, Takashi Nakashima, Yoshimitsu Kakuta, Kouhei Tsumoto, Makoto Kimura

Molecular Biosciences

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

5 Citations (Scopus)

Abstract

The protein component PhoRpp38 of Pyrococcus horikoshii ribonuclease P (RNase P) is known to be a multifunctional RNA-binding protein. Previous biochemical data indicate that it binds to two stem-loops in RNase P RNA (PhopRNA). Thermodynamic analysis revealed that PhoRpp38 and PhopRNA interact with each other with an association constant (Ka) of 1.56 × 10 ⁷ M ^-1. It was further found that PhoRpp38 simultaneously binds two stem-loop structures in PhopRNA with approximately equal affinity. Crystals of PhoRpp38 in complex with the stem-loop were grown and diffracted to a resolution of 7.0Å on a synchrotron X-ray source.

Original language	English
Pages (from-to)	1252-1255
Number of pages	4
Journal	Bioscience, Biotechnology and Biochemistry
Volume	76
Issue number	6
DOIs	https://doi.org/10.1271/bbb.120272
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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10.1271/bbb.120272

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title = "Thermodynamic analysis of a multifunctional RNA-binding protein, PhoRpp38, in the hyperthermophilic archaeon Pyrococcus horikoshii OT3",

abstract = "The protein component PhoRpp38 of Pyrococcus horikoshii ribonuclease P (RNase P) is known to be a multifunctional RNA-binding protein. Previous biochemical data indicate that it binds to two stem-loops in RNase P RNA (PhopRNA). Thermodynamic analysis revealed that PhoRpp38 and PhopRNA interact with each other with an association constant (Ka) of 1.56 × 10 7 M -1. It was further found that PhoRpp38 simultaneously binds two stem-loop structures in PhopRNA with approximately equal affinity. Crystals of PhoRpp38 in complex with the stem-loop were grown and diffracted to a resolution of 7.0{\AA} on a synchrotron X-ray source.",

author = "Kosuke Oshima and Takashi Nakashima and Yoshimitsu Kakuta and Kouhei Tsumoto and Makoto Kimura",

note = "Funding Information: We thank the staff of Spring-8 for their assistance in collecting data. Thanks are due to the Instrument Center of the Institute for Molecular Science for assistance in running the ITC experiments. This work was performed using a synchrotron beamline BL44XU at SPring-8 under the Cooperative Research Program of the Institute for Protein Research of Osaka University (Proposal nos. 2011A6618 and 2011B6618). It was supported in part 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).",

year = "2012",

doi = "10.1271/bbb.120272",

language = "English",

volume = "76",

pages = "1252--1255",

journal = "Bioscience, Biotechnology and Biochemistry",

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publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

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T1 - Thermodynamic analysis of a multifunctional RNA-binding protein, PhoRpp38, in the hyperthermophilic archaeon Pyrococcus horikoshii OT3

AU - Oshima, Kosuke

AU - Nakashima, Takashi

AU - Kakuta, Yoshimitsu

AU - Tsumoto, Kouhei

AU - Kimura, Makoto

N1 - Funding Information: We thank the staff of Spring-8 for their assistance in collecting data. Thanks are due to the Instrument Center of the Institute for Molecular Science for assistance in running the ITC experiments. This work was performed using a synchrotron beamline BL44XU at SPring-8 under the Cooperative Research Program of the Institute for Protein Research of Osaka University (Proposal nos. 2011A6618 and 2011B6618). It was supported in part 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 protein component PhoRpp38 of Pyrococcus horikoshii ribonuclease P (RNase P) is known to be a multifunctional RNA-binding protein. Previous biochemical data indicate that it binds to two stem-loops in RNase P RNA (PhopRNA). Thermodynamic analysis revealed that PhoRpp38 and PhopRNA interact with each other with an association constant (Ka) of 1.56 × 10 7 M -1. It was further found that PhoRpp38 simultaneously binds two stem-loop structures in PhopRNA with approximately equal affinity. Crystals of PhoRpp38 in complex with the stem-loop were grown and diffracted to a resolution of 7.0Å on a synchrotron X-ray source.

AB - The protein component PhoRpp38 of Pyrococcus horikoshii ribonuclease P (RNase P) is known to be a multifunctional RNA-binding protein. Previous biochemical data indicate that it binds to two stem-loops in RNase P RNA (PhopRNA). Thermodynamic analysis revealed that PhoRpp38 and PhopRNA interact with each other with an association constant (Ka) of 1.56 × 10 7 M -1. It was further found that PhoRpp38 simultaneously binds two stem-loop structures in PhopRNA with approximately equal affinity. Crystals of PhoRpp38 in complex with the stem-loop were grown and diffracted to a resolution of 7.0Å on a synchrotron X-ray source.

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JO - Bioscience, Biotechnology and Biochemistry

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Thermodynamic analysis of a multifunctional RNA-binding protein, PhoRpp38, in the hyperthermophilic archaeon Pyrococcus horikoshii OT3

Abstract

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