Viral macro domains reverse protein ADP-ribosylation.

ADP-ribosylation is a posttranslational protein modification in which ADP-ribose is transferred from NAD+ to specific acceptors to regulate a wide variety of cellular processes. The macro domain is an ancient and highly evolutionarily conserved protein domain widely distributed throughout all kingdo...

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मुख्य लेखकों: Li, C, Debing, Y, Jankevicius, G, Neyts, J, Ahel, I, Coutard, B, Canard, B
स्वरूप: Journal article
भाषा:English
प्रकाशित: American Society for Microbiology 2016
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author Li, C
Debing, Y
Jankevicius, G
Neyts, J
Ahel, I
Coutard, B
Canard, B
author_facet Li, C
Debing, Y
Jankevicius, G
Neyts, J
Ahel, I
Coutard, B
Canard, B
author_sort Li, C
collection OXFORD
description ADP-ribosylation is a posttranslational protein modification in which ADP-ribose is transferred from NAD+ to specific acceptors to regulate a wide variety of cellular processes. The macro domain is an ancient and highly evolutionarily conserved protein domain widely distributed throughout all kingdoms of life, including viruses. The human TARG1/C6orf130, MacroD1, and MacroD2 proteins can reverse ADP-ribosylation by acting on ADP-ribosylated substrates through the hydrolytic activity of their macro domains. Here, we report that the macro domain from hepatitis E virus (HEV) serves as an ADP-ribose-protein hydrolase for mono-ADP-ribose (MAR) and poly(ADP-ribose) (PAR) chain removal (de-MARylation and de-PARylation, respectively) from mono- and poly(ADP)-ribosylated proteins, respectively. The presence of the HEV helicase incisdramatically increases the binding of the macro domain to poly(ADP-ribose) and stimulates the de-PARylation activity. Abrogation of the latter dramatically decreases replication of an HEV subgenomic replicon. The de-MARylation activity is present in all three pathogenic positive-sense, single-stranded RNA [(+)ssRNA] virus families which carry a macro domain:Coronaviridae(severe acute respiratory syndrome coronavirus and human coronavirus 229E),Togaviridae(Venezuelan equine encephalitis virus), andHepeviridae (HEV), indicating that it might be a significant tropism and/or pathogenic determinant.
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spelling oxford-uuid:a8f05972-f2d5-4d20-bfef-e74050a5eb302022-03-27T03:05:04ZViral macro domains reverse protein ADP-ribosylation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:a8f05972-f2d5-4d20-bfef-e74050a5eb30EnglishSymplectic Elements at OxfordAmerican Society for Microbiology2016Li, CDebing, YJankevicius, GNeyts, JAhel, ICoutard, BCanard, BADP-ribosylation is a posttranslational protein modification in which ADP-ribose is transferred from NAD+ to specific acceptors to regulate a wide variety of cellular processes. The macro domain is an ancient and highly evolutionarily conserved protein domain widely distributed throughout all kingdoms of life, including viruses. The human TARG1/C6orf130, MacroD1, and MacroD2 proteins can reverse ADP-ribosylation by acting on ADP-ribosylated substrates through the hydrolytic activity of their macro domains. Here, we report that the macro domain from hepatitis E virus (HEV) serves as an ADP-ribose-protein hydrolase for mono-ADP-ribose (MAR) and poly(ADP-ribose) (PAR) chain removal (de-MARylation and de-PARylation, respectively) from mono- and poly(ADP)-ribosylated proteins, respectively. The presence of the HEV helicase incisdramatically increases the binding of the macro domain to poly(ADP-ribose) and stimulates the de-PARylation activity. Abrogation of the latter dramatically decreases replication of an HEV subgenomic replicon. The de-MARylation activity is present in all three pathogenic positive-sense, single-stranded RNA [(+)ssRNA] virus families which carry a macro domain:Coronaviridae(severe acute respiratory syndrome coronavirus and human coronavirus 229E),Togaviridae(Venezuelan equine encephalitis virus), andHepeviridae (HEV), indicating that it might be a significant tropism and/or pathogenic determinant.
spellingShingle Li, C
Debing, Y
Jankevicius, G
Neyts, J
Ahel, I
Coutard, B
Canard, B
Viral macro domains reverse protein ADP-ribosylation.
title Viral macro domains reverse protein ADP-ribosylation.
title_full Viral macro domains reverse protein ADP-ribosylation.
title_fullStr Viral macro domains reverse protein ADP-ribosylation.
title_full_unstemmed Viral macro domains reverse protein ADP-ribosylation.
title_short Viral macro domains reverse protein ADP-ribosylation.
title_sort viral macro domains reverse protein adp ribosylation
work_keys_str_mv AT lic viralmacrodomainsreverseproteinadpribosylation
AT debingy viralmacrodomainsreverseproteinadpribosylation
AT jankeviciusg viralmacrodomainsreverseproteinadpribosylation
AT neytsj viralmacrodomainsreverseproteinadpribosylation
AT aheli viralmacrodomainsreverseproteinadpribosylation
AT coutardb viralmacrodomainsreverseproteinadpribosylation
AT canardb viralmacrodomainsreverseproteinadpribosylation