Structural modeling of RNase P RNA of the hyperthermophilic archaeon Pyrococcus horikoshii OT3

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Structural modeling of RNase P RNA of the hyperthermophilic archaeon Pyrococcus horikoshii OT3. / Zwieb, C.; Nakao, Y.; Nakashima, T.; Takagi, H.; Goda, S.; Andersen, E.S.; Kakuta, Y.; Kimura, M.

In: Biochemical and Biophysical Research Communications, Vol. 414, No. 3, 28.10.2011, p. 517-522.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Zwieb, C, Nakao, Y, Nakashima, T, Takagi, H, Goda, S, Andersen, ES, Kakuta, Y & Kimura, M 2011, 'Structural modeling of RNase P RNA of the hyperthermophilic archaeon Pyrococcus horikoshii OT3', Biochemical and Biophysical Research Communications, vol. 414, no. 3, pp. 517-522. https://doi.org/10.1016/j.bbrc.2011.09.098

APA

Zwieb, C., Nakao, Y., Nakashima, T., Takagi, H., Goda, S., Andersen, E. S., ... Kimura, M. (2011). Structural modeling of RNase P RNA of the hyperthermophilic archaeon Pyrococcus horikoshii OT3. Biochemical and Biophysical Research Communications, 414(3), 517-522. https://doi.org/10.1016/j.bbrc.2011.09.098

CBE

Zwieb C, Nakao Y, Nakashima T, Takagi H, Goda S, Andersen ES, Kakuta Y, Kimura M. 2011. Structural modeling of RNase P RNA of the hyperthermophilic archaeon Pyrococcus horikoshii OT3. Biochemical and Biophysical Research Communications. 414(3):517-522. https://doi.org/10.1016/j.bbrc.2011.09.098

MLA

Zwieb, C. et al. "Structural modeling of RNase P RNA of the hyperthermophilic archaeon Pyrococcus horikoshii OT3". Biochemical and Biophysical Research Communications. 2011, 414(3). 517-522. https://doi.org/10.1016/j.bbrc.2011.09.098

Vancouver

Zwieb C, Nakao Y, Nakashima T, Takagi H, Goda S, Andersen ES et al. Structural modeling of RNase P RNA of the hyperthermophilic archaeon Pyrococcus horikoshii OT3. Biochemical and Biophysical Research Communications. 2011 Oct 28;414(3):517-522. https://doi.org/10.1016/j.bbrc.2011.09.098

Author

Zwieb, C. ; Nakao, Y. ; Nakashima, T. ; Takagi, H. ; Goda, S. ; Andersen, E.S. ; Kakuta, Y. ; Kimura, M. / Structural modeling of RNase P RNA of the hyperthermophilic archaeon Pyrococcus horikoshii OT3. In: Biochemical and Biophysical Research Communications. 2011 ; Vol. 414, No. 3. pp. 517-522.

Bibtex

@article{e77d9b7521f440749c6450dfc9e5a08f,
title = "Structural modeling of RNase P RNA of the hyperthermophilic archaeon Pyrococcus horikoshii OT3",
abstract = "Ribonuclease P (RNase P) is a ubiquitous trans-acting ribozyme that processes the 5' leader sequence of precursor tRNA (pre-tRNA). The RNase P RNA (PhopRNA) of the hyperthermophilic archaeon Pyrococcus horikoshii OT3 is central to the catalytic process and binds five proteins (PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38) which contribute to the enzymatic activity of the holoenzyme. Despite significant progress in determining the crystal structure of the proteins, the structure of PhopRNA remains elusive. Comparative analysis of the RNase P RNA sequences and existing crystallographic structural information of the bacterial RNase P RNAs were combined to generate a phylogenetically supported three-dimensional (3-D) model of the PhopRNA. The model structure shows an essentially flat disk with 16 tightly packed helices and a conserved face suitable for the binding of pre-tRNA. Moreover, the structure in solution was investigated by enzymatic probing and small-angle X-ray scattering (SAXS) analysis. The low resolution model derived from SAXS and the comparative 3-D model have similar overall shapes. The 3-D model provides a framework for a better understanding of structure-function relationships of this multifaceted primordial ribozyme.",
author = "C. Zwieb and Y. Nakao and T. Nakashima and H. Takagi and S. Goda and E.S. Andersen and Y. Kakuta and M. Kimura",
note = "MEDLINE{\circledR} is the source for the MeSH terms of this document.",
year = "2011",
month = "10",
day = "28",
doi = "10.1016/j.bbrc.2011.09.098",
language = "English",
volume = "414",
pages = "517--522",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier Inc",
number = "3",

}

RIS

TY - JOUR

T1 - Structural modeling of RNase P RNA of the hyperthermophilic archaeon Pyrococcus horikoshii OT3

AU - Zwieb, C.

AU - Nakao, Y.

AU - Nakashima, T.

AU - Takagi, H.

AU - Goda, S.

AU - Andersen, E.S.

AU - Kakuta, Y.

AU - Kimura, M.

N1 - MEDLINE® is the source for the MeSH terms of this document.

PY - 2011/10/28

Y1 - 2011/10/28

N2 - Ribonuclease P (RNase P) is a ubiquitous trans-acting ribozyme that processes the 5' leader sequence of precursor tRNA (pre-tRNA). The RNase P RNA (PhopRNA) of the hyperthermophilic archaeon Pyrococcus horikoshii OT3 is central to the catalytic process and binds five proteins (PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38) which contribute to the enzymatic activity of the holoenzyme. Despite significant progress in determining the crystal structure of the proteins, the structure of PhopRNA remains elusive. Comparative analysis of the RNase P RNA sequences and existing crystallographic structural information of the bacterial RNase P RNAs were combined to generate a phylogenetically supported three-dimensional (3-D) model of the PhopRNA. The model structure shows an essentially flat disk with 16 tightly packed helices and a conserved face suitable for the binding of pre-tRNA. Moreover, the structure in solution was investigated by enzymatic probing and small-angle X-ray scattering (SAXS) analysis. The low resolution model derived from SAXS and the comparative 3-D model have similar overall shapes. The 3-D model provides a framework for a better understanding of structure-function relationships of this multifaceted primordial ribozyme.

AB - Ribonuclease P (RNase P) is a ubiquitous trans-acting ribozyme that processes the 5' leader sequence of precursor tRNA (pre-tRNA). The RNase P RNA (PhopRNA) of the hyperthermophilic archaeon Pyrococcus horikoshii OT3 is central to the catalytic process and binds five proteins (PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38) which contribute to the enzymatic activity of the holoenzyme. Despite significant progress in determining the crystal structure of the proteins, the structure of PhopRNA remains elusive. Comparative analysis of the RNase P RNA sequences and existing crystallographic structural information of the bacterial RNase P RNAs were combined to generate a phylogenetically supported three-dimensional (3-D) model of the PhopRNA. The model structure shows an essentially flat disk with 16 tightly packed helices and a conserved face suitable for the binding of pre-tRNA. Moreover, the structure in solution was investigated by enzymatic probing and small-angle X-ray scattering (SAXS) analysis. The low resolution model derived from SAXS and the comparative 3-D model have similar overall shapes. The 3-D model provides a framework for a better understanding of structure-function relationships of this multifaceted primordial ribozyme.

UR - http://www.scopus.com/inward/record.url?scp=80054878573&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2011.09.098

DO - 10.1016/j.bbrc.2011.09.098

M3 - Journal article

C2 - 21968019

AN - SCOPUS:80054878573

VL - 414

SP - 517

EP - 522

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -