Archaeal RNA polymerase: The influence of the protruding stalk in crystal packing and preliminary biophysical analysis of the Rpo13 subunit

Magdalena Wojtas; Bibiana Peralta; Marina Ondiviela; Maria Mogni; Stephen D. Bell; Nicola G.A. Abrescia

doi:10.1042/BST0390025

Archaeal RNA polymerase: The influence of the protruding stalk in crystal packing and preliminary biophysical analysis of the Rpo13 subunit

Magdalena Wojtas, Bibiana Peralta, Marina Ondiviela, Maria Mogni, Stephen D. Bell, Nicola G.A. Abrescia

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

9 Scopus citations

Abstract

We review recent results on the complete structure of the archaeal RNAP (RNA polymerase) enzyme of Sulfolobus shibatae. We compare the three crystal forms in which this RNAP packs (space groups P2₁2₁2 ₁, P2₁2₁2 and P2₁) and provide a preliminary biophysical characterization of the newly identified 13-subunit Rpo13. The availability of different crystal forms for this RNAP allows the analysis of the packing degeneracy and the intermolecular interactions that determine this degeneracy. We observe the pivotal role played by the protruding stalk composed of subunits Rpo4 and Rpo7 in the lattice contacts. Aided by MALLS (multi-angle laser light scattering), we have initiated the biophysical characterization of the recombinantly expressed and purified subunit Rpo13, a necessary step towards the understanding of Rpo13's role in archaeal transcription.

Original language	English
Pages (from-to)	25-30
Number of pages	6
Journal	Biochemical Society Transactions
Volume	39
Issue number	1
DOIs	https://doi.org/10.1042/BST0390025
State	Published - 1 Feb 2011
Externally published	Yes

Keywords

Archaeon
RNA polymerase
Rpo13
Transcription
X-ray structure

ASJC Scopus subject areas

Biochemistry

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10.1042/BST0390025

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title = "Archaeal RNA polymerase: The influence of the protruding stalk in crystal packing and preliminary biophysical analysis of the Rpo13 subunit",

abstract = "We review recent results on the complete structure of the archaeal RNAP (RNA polymerase) enzyme of Sulfolobus shibatae. We compare the three crystal forms in which this RNAP packs (space groups P21212 1, P21212 and P21) and provide a preliminary biophysical characterization of the newly identified 13-subunit Rpo13. The availability of different crystal forms for this RNAP allows the analysis of the packing degeneracy and the intermolecular interactions that determine this degeneracy. We observe the pivotal role played by the protruding stalk composed of subunits Rpo4 and Rpo7 in the lattice contacts. Aided by MALLS (multi-angle laser light scattering), we have initiated the biophysical characterization of the recombinantly expressed and purified subunit Rpo13, a necessary step towards the understanding of Rpo13's role in archaeal transcription.",

keywords = "Archaeon, RNA polymerase, Rpo13, Transcription, X-ray structure",

author = "Magdalena Wojtas and Bibiana Peralta and Marina Ondiviela and Maria Mogni and Bell, {Stephen D.} and Abrescia, {Nicola G.A.}",

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T2 - The influence of the protruding stalk in crystal packing and preliminary biophysical analysis of the Rpo13 subunit

AU - Wojtas, Magdalena

AU - Peralta, Bibiana

AU - Ondiviela, Marina

AU - Mogni, Maria

AU - Bell, Stephen D.

AU - Abrescia, Nicola G.A.

PY - 2011/2/1

Y1 - 2011/2/1

N2 - We review recent results on the complete structure of the archaeal RNAP (RNA polymerase) enzyme of Sulfolobus shibatae. We compare the three crystal forms in which this RNAP packs (space groups P21212 1, P21212 and P21) and provide a preliminary biophysical characterization of the newly identified 13-subunit Rpo13. The availability of different crystal forms for this RNAP allows the analysis of the packing degeneracy and the intermolecular interactions that determine this degeneracy. We observe the pivotal role played by the protruding stalk composed of subunits Rpo4 and Rpo7 in the lattice contacts. Aided by MALLS (multi-angle laser light scattering), we have initiated the biophysical characterization of the recombinantly expressed and purified subunit Rpo13, a necessary step towards the understanding of Rpo13's role in archaeal transcription.

AB - We review recent results on the complete structure of the archaeal RNAP (RNA polymerase) enzyme of Sulfolobus shibatae. We compare the three crystal forms in which this RNAP packs (space groups P21212 1, P21212 and P21) and provide a preliminary biophysical characterization of the newly identified 13-subunit Rpo13. The availability of different crystal forms for this RNAP allows the analysis of the packing degeneracy and the intermolecular interactions that determine this degeneracy. We observe the pivotal role played by the protruding stalk composed of subunits Rpo4 and Rpo7 in the lattice contacts. Aided by MALLS (multi-angle laser light scattering), we have initiated the biophysical characterization of the recombinantly expressed and purified subunit Rpo13, a necessary step towards the understanding of Rpo13's role in archaeal transcription.

KW - Archaeon

KW - RNA polymerase

KW - Rpo13

KW - Transcription

KW - X-ray structure

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JF - Biochemical Society Transactions

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Archaeal RNA polymerase: The influence of the protruding stalk in crystal packing and preliminary biophysical analysis of the Rpo13 subunit

Abstract

Keywords

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