CovidV2, PascalFrancis, Curation, bibRecord, 000019

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

Identifieur interne : 000019 ( PascalFrancis/Curation ); précédent : 000018; suivant : 000020

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

Auteurs : Marie-Pierre Egloff [France] ; Hélène Malet [France] ; Akos Putics [Allemagne] ; Maarit Heinonen [Finlande] ; Hélène Dutartre [France] ; Antoine Frangeui [France] ; Arnaud Gruez [France] ; Valérie Campanacci [France] ; Christian Cambillau [France] ; John Ziebuhr [Allemagne, Royaume-Uni] ; Tero Ahola [Finlande] ; Bruno Canard [France]

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.

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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.`
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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`
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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`

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Pascal:06-0412132

Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains</title>
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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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