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Title: Expression, purification, crystallization and preliminary crystallographic study of isolated modules of the mouse coactivator-associated arginine methyltransferase 1

Abstract

Isolated modules of mouse coactivator-associated arginine methyltransferase 1 encompassing the protein arginine N-methyltransferase catalytic domain have been overexpressed, purified and crystallized. X-ray diffraction data have been collected and have enabled determination of the structures by multiple isomorphous replacement using anomalous scattering. Coactivator-associated arginine methyltransferase 1 (CARM1) plays a crucial role in gene expression as a coactivator of several nuclear hormone receptors and also of non-nuclear receptor systems. Its recruitment by the transcriptional machinery induces protein methylation, leading to chromatin remodelling and gene activation. CARM1{sub 28–507} and two structural states of CARM1{sub 140–480} were expressed, purified and crystallized. Crystals of CARM1{sub 28–507} belong to space group P6{sub 2}22, with unit-cell parameters a = b = 136.0, c = 125.3 Å; they diffract to beyond 2.5 Å resolution using synchrotron radiation and contain one monomer in the asymmetric unit. The structure of CARM1{sub 28–507} was solved by multiple isomorphous replacement and anomalous scattering methods. Crystals of apo CARM1{sub 140–480} belong to space group I222, with unit-cell parameters a = 74.6, b = 99.0, c = 207.4 Å; they diffract to beyond 2.7 Å resolution and contain two monomers in the asymmetric unit. Crystals of CARM1{sub 140–480} in complex with S-adenosyl-l-homocysteine belong tomore » space P2{sub 1}2{sub 1}2, with unit-cell parameters a = 74.6, b = 98.65, c = 206.08 Å; they diffract to beyond 2.6 Å resolution and contain four monomers in the asymmetric unit. The structures of apo and holo CARM1{sub 140–480} were solved by molecular-replacement techniques from the structure of CARM1{sub 28–507}.« less

Authors:
; ; ; ;  [1];  [2];  [2];  [2]
  1. IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire), Département de Biologie et Génomique Structurales, 1 Rue Laurent Fries, Illkirch, F-67404 (France)
  2. (France)
Publication Date:
OSTI Identifier:
22360297
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 4; Other Information: PMCID: PMC2330207; PMID: 17401209; PUBLISHER-ID: fw5131; OAI: oai:pubmedcentral.nih.gov:2330207; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ARGININE; CRYSTALLIZATION; CRYSTALS; MONOMERS; RECEPTORS; RESOLUTION; SPACE GROUPS; SYNCHROTRON RADIATION; X-RAY DIFFRACTION

Citation Formats

Troffer-Charlier, Nathalie, Cura, Vincent, Hassenboehler, Pierre, Moras, Dino, Cavarelli, Jean, E-mail: cava@igbmc.u-strasbg.fr, INSERM, U596, Illkirch, F-67400, CNRS, UMR7104, Illkirch, F-67400, and Université Louis Pasteur, Faculté des Sciences de la Vie, Strasbourg, F-67000. Expression, purification, crystallization and preliminary crystallographic study of isolated modules of the mouse coactivator-associated arginine methyltransferase 1. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107011785.
Troffer-Charlier, Nathalie, Cura, Vincent, Hassenboehler, Pierre, Moras, Dino, Cavarelli, Jean, E-mail: cava@igbmc.u-strasbg.fr, INSERM, U596, Illkirch, F-67400, CNRS, UMR7104, Illkirch, F-67400, & Université Louis Pasteur, Faculté des Sciences de la Vie, Strasbourg, F-67000. Expression, purification, crystallization and preliminary crystallographic study of isolated modules of the mouse coactivator-associated arginine methyltransferase 1. United Kingdom. doi:10.1107/S1744309107011785.
Troffer-Charlier, Nathalie, Cura, Vincent, Hassenboehler, Pierre, Moras, Dino, Cavarelli, Jean, E-mail: cava@igbmc.u-strasbg.fr, INSERM, U596, Illkirch, F-67400, CNRS, UMR7104, Illkirch, F-67400, and Université Louis Pasteur, Faculté des Sciences de la Vie, Strasbourg, F-67000. Sun . "Expression, purification, crystallization and preliminary crystallographic study of isolated modules of the mouse coactivator-associated arginine methyltransferase 1". United Kingdom. doi:10.1107/S1744309107011785.
@article{osti_22360297,
title = {Expression, purification, crystallization and preliminary crystallographic study of isolated modules of the mouse coactivator-associated arginine methyltransferase 1},
author = {Troffer-Charlier, Nathalie and Cura, Vincent and Hassenboehler, Pierre and Moras, Dino and Cavarelli, Jean, E-mail: cava@igbmc.u-strasbg.fr and INSERM, U596, Illkirch, F-67400 and CNRS, UMR7104, Illkirch, F-67400 and Université Louis Pasteur, Faculté des Sciences de la Vie, Strasbourg, F-67000},
abstractNote = {Isolated modules of mouse coactivator-associated arginine methyltransferase 1 encompassing the protein arginine N-methyltransferase catalytic domain have been overexpressed, purified and crystallized. X-ray diffraction data have been collected and have enabled determination of the structures by multiple isomorphous replacement using anomalous scattering. Coactivator-associated arginine methyltransferase 1 (CARM1) plays a crucial role in gene expression as a coactivator of several nuclear hormone receptors and also of non-nuclear receptor systems. Its recruitment by the transcriptional machinery induces protein methylation, leading to chromatin remodelling and gene activation. CARM1{sub 28–507} and two structural states of CARM1{sub 140–480} were expressed, purified and crystallized. Crystals of CARM1{sub 28–507} belong to space group P6{sub 2}22, with unit-cell parameters a = b = 136.0, c = 125.3 Å; they diffract to beyond 2.5 Å resolution using synchrotron radiation and contain one monomer in the asymmetric unit. The structure of CARM1{sub 28–507} was solved by multiple isomorphous replacement and anomalous scattering methods. Crystals of apo CARM1{sub 140–480} belong to space group I222, with unit-cell parameters a = 74.6, b = 99.0, c = 207.4 Å; they diffract to beyond 2.7 Å resolution and contain two monomers in the asymmetric unit. Crystals of CARM1{sub 140–480} in complex with S-adenosyl-l-homocysteine belong to space P2{sub 1}2{sub 1}2, with unit-cell parameters a = 74.6, b = 98.65, c = 206.08 Å; they diffract to beyond 2.6 Å resolution and contain four monomers in the asymmetric unit. The structures of apo and holo CARM1{sub 140–480} were solved by molecular-replacement techniques from the structure of CARM1{sub 28–507}.},
doi = {10.1107/S1744309107011785},
journal = {Acta Crystallographica. Section F},
number = Pt 4,
volume = 63,
place = {United Kingdom},
year = {Sun Apr 01 00:00:00 EDT 2007},
month = {Sun Apr 01 00:00:00 EDT 2007}
}