CovidV2, PascalFrancis, Corpus, bibRecord, 000040

Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains

Identifieur interne : 000040 ( PascalFrancis/Corpus ); précédent : 000039; suivant : 000041

Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains

Auteurs : Marie-Pierre Egloff ; Hélène Malet ; Akos Putics ; Maarit Heinonen ; Hélène Dutartre ; Antoine Frangeui ; Arnaud Gruez ; Valérie Campanacci ; Christian Cambillau ; John Ziebuhr ; Tero Ahola ; Bruno Canard

Source :

Journal of virology [ 0022-538X ] ; 2006.

RBID : Pascal:06-0412132

Descripteurs français

Pascal (Inist)
- ADP, Microbiologie, Virologie.

English descriptors

KwdEn :
- ADP, Microbiology, Virology.

Abstract

Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Å resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly-(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A08	`01`	`1`	`ENG`	`@1 Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains`
A11	`01`	`1`		`@1 EGLOFF (Marie-Pierre)`
A11	`02`	`1`		`@1 MALET (Hélène)`
A11	`03`	`1`		`@1 PUTICS (Akos)`
A11	`04`	`1`		`@1 HEINONEN (Maarit)`
A11	`05`	`1`		`@1 DUTARTRE (Hélène)`
A11	`06`	`1`		`@1 FRANGEUI (Antoine)`
A11	`07`	`1`		`@1 GRUEZ (Arnaud)`
A11	`08`	`1`		`@1 CAMPANACCI (Valérie)`
A11	`09`	`1`		`@1 CAMBILLAU (Christian)`
A11	`10`	`1`		`@1 ZIEBUHR (John)`
A11	`11`	`1`		`@1 AHOLA (Tero)`
A11	`12`	`1`		`@1 CANARD (Bruno)`
A14	`01`			`@1 Centre National de la Recherche Scientifique and Universités d'Aix-Marseille I et II, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Ecole Supérieure d'lngénieurs de Luminy-Case 925, 163 Ave. de Luminy @2 13288 Marseille @3 FRA @Z 1 aut. @Z 2 aut. @Z 5 aut. @Z 6 aut. @Z 7 aut. @Z 8 aut. @Z 9 aut. @Z 12 aut.`
A14	`02`			`@1 Institute of Virology and Immunology, University of Wilrzburg, Versbacher Strasse 7 @2 97078 Würzburg @3 DEU @Z 3 aut. @Z 10 aut.`
A14	`03`			`@1 Program in Cellular Biotechnology, Institute of Biotechnology, University of Helsinki, P.O. Box 56, Viikinkaari 9 @2 00014 Helsinki @3 FIN @Z 4 aut. @Z 11 aut.`
A14	`04`			`@1 Centre for Cancer Research and Cell Biology, School of Biomedical Sciences, The Queen's University of Belfast, 97 Lisbum Rd @2 Belfast BT9 7BL @3 GBR @Z 10 aut.`
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A44				`@0 0000 @1 © 2006 INIST-CNRS. All rights reserved.`
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A64	`01`	`1`		`@0 Journal of virology`
A66	`01`			`@0 USA`
C01	`01`		`ENG`	@0 Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Å resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly-(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.
C02	`01`	`X`		`@0 002A05C10`
C03	`01`	`X`	`FRE`	`@0 ADP @2 NK @5 05`
C03	`01`	`X`	`ENG`	`@0 ADP @2 NK @5 05`
C03	`01`	`X`	`SPA`	`@0 ADP @2 NK @5 05`
C03	`02`	`X`	`FRE`	`@0 Microbiologie @5 06`
C03	`02`	`X`	`ENG`	`@0 Microbiology @5 06`
C03	`02`	`X`	`SPA`	`@0 Microbiología @5 06`
C03	`03`	`X`	`FRE`	`@0 Virologie @5 07`
C03	`03`	`X`	`ENG`	`@0 Virology @5 07`
C03	`03`	`X`	`SPA`	`@0 Virología @5 07`
N21				`@1 275`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

Format Inist (serveur)

NO :	PASCAL 06-0412132 INIST
ET :	Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains
AU :	EGLOFF (Marie-Pierre); MALET (Hélène); PUTICS (Akos); HEINONEN (Maarit); DUTARTRE (Hélène); FRANGEUI (Antoine); GRUEZ (Arnaud); CAMPANACCI (Valérie); CAMBILLAU (Christian); ZIEBUHR (John); AHOLA (Tero); CANARD (Bruno)
AF :	Centre National de la Recherche Scientifique and Universités d'Aix-Marseille I et II, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Ecole Supérieure d'lngénieurs de Luminy-Case 925, 163 Ave. de Luminy/13288 Marseille/France (1 aut., 2 aut., 5 aut., 6 aut., 7 aut., 8 aut., 9 aut., 12 aut.); Institute of Virology and Immunology, University of Wilrzburg, Versbacher Strasse 7/97078 Würzburg/Allemagne (3 aut., 10 aut.); Program in Cellular Biotechnology, Institute of Biotechnology, University of Helsinki, P.O. Box 56, Viikinkaari 9/00014 Helsinki/Finlande (4 aut., 11 aut.); Centre for Cancer Research and Cell Biology, School of Biomedical Sciences, The Queen's University of Belfast, 97 Lisbum Rd/Belfast BT9 7BL/Royaume-Uni (10 aut.)
DT :	Publication en série; Niveau analytique
SO :	Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2006; Vol. 80; No. 17; Pp. 8493-8502; Bibl. 43 ref.
LA :	Anglais
EA :	Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Å resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly-(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.
CC :	002A05C10
FD :	ADP; Microbiologie; Virologie
ED :	ADP; Microbiology; Virology
SD :	ADP; Microbiología; Virología
LO :	INIST-13592.354000133520840190
ID :	06-0412132

Links to Exploration step

Pascal:06-0412132

Le document en format XML

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<author><name sortKey="Gruez, Arnaud" sort="Gruez, Arnaud" uniqKey="Gruez A" first="Arnaud" last="Gruez">Arnaud Gruez</name>
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<front><div type="abstract" xml:lang="en">Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Å resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly-(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.</div>
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<AU>EGLOFF (Marie-Pierre); MALET (Hélène); PUTICS (Akos); HEINONEN (Maarit); DUTARTRE (Hélène); FRANGEUI (Antoine); GRUEZ (Arnaud); CAMPANACCI (Valérie); CAMBILLAU (Christian); ZIEBUHR (John); AHOLA (Tero); CANARD (Bruno)</AU>
<AF>Centre National de la Recherche Scientifique and Universités d'Aix-Marseille I et II, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Ecole Supérieure d'lngénieurs de Luminy-Case 925, 163 Ave. de Luminy/13288 Marseille/France (1 aut., 2 aut., 5 aut., 6 aut., 7 aut., 8 aut., 9 aut., 12 aut.); Institute of Virology and Immunology, University of Wilrzburg, Versbacher Strasse 7/97078 Würzburg/Allemagne (3 aut., 10 aut.); Program in Cellular Biotechnology, Institute of Biotechnology, University of Helsinki, P.O. Box 56, Viikinkaari 9/00014 Helsinki/Finlande (4 aut., 11 aut.); Centre for Cancer Research and Cell Biology, School of Biomedical Sciences, The Queen's University of Belfast, 97 Lisbum Rd/Belfast BT9 7BL/Royaume-Uni (10 aut.)</AF>
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Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains

Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains

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