Structural biology of the ribonuclease p in the hyperthermophilic archaeon pyrococcus horikoshii OT3

Makoto Kimura, Yoshimitsu Kakuta

研究成果: 著書/レポートタイプへの貢献

6 引用 (Scopus)

抄録

Pyrococcus horikoshii OT3 is a hyperthermophilic archaeaon -isolated from hydrothermal fluid. Because of their genetic features as well as hyperthermophilic properties, macromolecules produced by this thermophilic bacterium have served as an excellent model for structural biology. Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5′-leader sequence of precursor tRNA (pre-tRNA). We found that RNase P RNA (PhopRNA) and five proteins in P. horikoshii OT3 reconstituted RNase P activity that exhibited enzymatic properties like those of the authentic enzyme. A mutational analysis indicated that nucleotides A40, A41, and U44 in PhopRNA are crucial for catalysis, strongly suggesting that PhopRNA catalyzes the hydrolysis of pre-tRNA in approximately the same manner as eubacterial RNase P RNAs, even though it has no enzymatic activity in the absence of the proteins. The P. horikoshii RNase P proteins are predominantly involved in optimization of PhopRNA's conformation, though individually they are dispensable for RNase P activity in vitro. This chapter summarizes structure-function relationships of the P. horikoshii RNase P subunits, including the high-resolution structural information that is currently available for the protein subunits.

元の言語英語
ホスト出版物のタイトルMicroorganisms in Sustainable Agriculture and Biotechnology
出版者Springer Netherlands
ページ487-508
ページ数22
9789400722149
ISBN(電子版)9789400722149
ISBN(印刷物)9400722133, 9789400722132
DOI
出版物ステータス出版済み - 10 1 2012

Fingerprint

Pyrococcus horikoshii
Ribonuclease P
Archaea
Ribonucleases
RNA Precursors
RNA
Proteins
Ribonucleoproteins
Structural Models
Protein Subunits
Catalysis
Hydrolysis
Nucleotides
Bacteria

All Science Journal Classification (ASJC) codes

  • Immunology and Microbiology(all)

これを引用

Kimura, M., & Kakuta, Y. (2012). Structural biology of the ribonuclease p in the hyperthermophilic archaeon pyrococcus horikoshii OT3. : Microorganisms in Sustainable Agriculture and Biotechnology (巻 9789400722149, pp. 487-508). Springer Netherlands. https://doi.org/10.1007/978-94-007-2214-9_23

Structural biology of the ribonuclease p in the hyperthermophilic archaeon pyrococcus horikoshii OT3. / Kimura, Makoto; Kakuta, Yoshimitsu.

Microorganisms in Sustainable Agriculture and Biotechnology. 巻 9789400722149 Springer Netherlands, 2012. p. 487-508.

研究成果: 著書/レポートタイプへの貢献

Kimura, M & Kakuta, Y 2012, Structural biology of the ribonuclease p in the hyperthermophilic archaeon pyrococcus horikoshii OT3. : Microorganisms in Sustainable Agriculture and Biotechnology. 巻. 9789400722149, Springer Netherlands, pp. 487-508. https://doi.org/10.1007/978-94-007-2214-9_23
Kimura M, Kakuta Y. Structural biology of the ribonuclease p in the hyperthermophilic archaeon pyrococcus horikoshii OT3. : Microorganisms in Sustainable Agriculture and Biotechnology. 巻 9789400722149. Springer Netherlands. 2012. p. 487-508 https://doi.org/10.1007/978-94-007-2214-9_23
Kimura, Makoto ; Kakuta, Yoshimitsu. / Structural biology of the ribonuclease p in the hyperthermophilic archaeon pyrococcus horikoshii OT3. Microorganisms in Sustainable Agriculture and Biotechnology. 巻 9789400722149 Springer Netherlands, 2012. pp. 487-508
@inbook{a201b682a4714ae3adcb802b89706713,
title = "Structural biology of the ribonuclease p in the hyperthermophilic archaeon pyrococcus horikoshii OT3",
abstract = "Pyrococcus horikoshii OT3 is a hyperthermophilic archaeaon -isolated from hydrothermal fluid. Because of their genetic features as well as hyperthermophilic properties, macromolecules produced by this thermophilic bacterium have served as an excellent model for structural biology. Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5′-leader sequence of precursor tRNA (pre-tRNA). We found that RNase P RNA (PhopRNA) and five proteins in P. horikoshii OT3 reconstituted RNase P activity that exhibited enzymatic properties like those of the authentic enzyme. A mutational analysis indicated that nucleotides A40, A41, and U44 in PhopRNA are crucial for catalysis, strongly suggesting that PhopRNA catalyzes the hydrolysis of pre-tRNA in approximately the same manner as eubacterial RNase P RNAs, even though it has no enzymatic activity in the absence of the proteins. The P. horikoshii RNase P proteins are predominantly involved in optimization of PhopRNA's conformation, though individually they are dispensable for RNase P activity in vitro. This chapter summarizes structure-function relationships of the P. horikoshii RNase P subunits, including the high-resolution structural information that is currently available for the protein subunits.",
author = "Makoto Kimura and Yoshimitsu Kakuta",
year = "2012",
month = "10",
day = "1",
doi = "10.1007/978-94-007-2214-9_23",
language = "English",
isbn = "9400722133",
volume = "9789400722149",
pages = "487--508",
booktitle = "Microorganisms in Sustainable Agriculture and Biotechnology",
publisher = "Springer Netherlands",
address = "Netherlands",

}

TY - CHAP

T1 - Structural biology of the ribonuclease p in the hyperthermophilic archaeon pyrococcus horikoshii OT3

AU - Kimura, Makoto

AU - Kakuta, Yoshimitsu

PY - 2012/10/1

Y1 - 2012/10/1

N2 - Pyrococcus horikoshii OT3 is a hyperthermophilic archaeaon -isolated from hydrothermal fluid. Because of their genetic features as well as hyperthermophilic properties, macromolecules produced by this thermophilic bacterium have served as an excellent model for structural biology. Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5′-leader sequence of precursor tRNA (pre-tRNA). We found that RNase P RNA (PhopRNA) and five proteins in P. horikoshii OT3 reconstituted RNase P activity that exhibited enzymatic properties like those of the authentic enzyme. A mutational analysis indicated that nucleotides A40, A41, and U44 in PhopRNA are crucial for catalysis, strongly suggesting that PhopRNA catalyzes the hydrolysis of pre-tRNA in approximately the same manner as eubacterial RNase P RNAs, even though it has no enzymatic activity in the absence of the proteins. The P. horikoshii RNase P proteins are predominantly involved in optimization of PhopRNA's conformation, though individually they are dispensable for RNase P activity in vitro. This chapter summarizes structure-function relationships of the P. horikoshii RNase P subunits, including the high-resolution structural information that is currently available for the protein subunits.

AB - Pyrococcus horikoshii OT3 is a hyperthermophilic archaeaon -isolated from hydrothermal fluid. Because of their genetic features as well as hyperthermophilic properties, macromolecules produced by this thermophilic bacterium have served as an excellent model for structural biology. Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5′-leader sequence of precursor tRNA (pre-tRNA). We found that RNase P RNA (PhopRNA) and five proteins in P. horikoshii OT3 reconstituted RNase P activity that exhibited enzymatic properties like those of the authentic enzyme. A mutational analysis indicated that nucleotides A40, A41, and U44 in PhopRNA are crucial for catalysis, strongly suggesting that PhopRNA catalyzes the hydrolysis of pre-tRNA in approximately the same manner as eubacterial RNase P RNAs, even though it has no enzymatic activity in the absence of the proteins. The P. horikoshii RNase P proteins are predominantly involved in optimization of PhopRNA's conformation, though individually they are dispensable for RNase P activity in vitro. This chapter summarizes structure-function relationships of the P. horikoshii RNase P subunits, including the high-resolution structural information that is currently available for the protein subunits.

UR - http://www.scopus.com/inward/record.url?scp=84906088324&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84906088324&partnerID=8YFLogxK

U2 - 10.1007/978-94-007-2214-9_23

DO - 10.1007/978-94-007-2214-9_23

M3 - Chapter

SN - 9400722133

SN - 9789400722132

VL - 9789400722149

SP - 487

EP - 508

BT - Microorganisms in Sustainable Agriculture and Biotechnology

PB - Springer Netherlands

ER -