A Flexible and Original Architecture of Two Unrelated Zinc Fingers Underlies the Role of the Multitask P1 in RYMV Spread
Vianney Poignavent
(1)
,
François Hoh
(2, 3)
,
Guillaume Terral
(4)
,
Yinshan Yang
(2, 3)
,
François-Xavier Gillet
(5)
,
Jeong-Hyeon Kim
(6)
,
Frédéric Allemand
(2, 3)
,
Eric Lacombe
(7)
,
Christophe Brugidou
(8)
,
Sarah Cianferani
(4)
,
Hélène Déméné
(2, 3)
,
Florence Vignols
(9)
1
IBMP -
Institut de Biologie Moléculaire des Plantes
2 CBS - Centre de Biologie Structurale [Montpellier]
3 BCM - BioCampus
4 LSMBO - Laboratoire de Spectrométrie de Masse BioOrganique [Strasbourg]
5 MAP - Microbiologie, adaptation et pathogénie
6 UMR IPME - UMR - Interactions Plantes Microorganismes Environnement
7 UMR DIADE - Diversité, adaptation, développement des plantes
8 UMR PHIM - Plant Health Institute of Montpellier
9 IPSIM - Institut des Sciences des Plantes de Montpellier
2 CBS - Centre de Biologie Structurale [Montpellier]
3 BCM - BioCampus
4 LSMBO - Laboratoire de Spectrométrie de Masse BioOrganique [Strasbourg]
5 MAP - Microbiologie, adaptation et pathogénie
6 UMR IPME - UMR - Interactions Plantes Microorganismes Environnement
7 UMR DIADE - Diversité, adaptation, développement des plantes
8 UMR PHIM - Plant Health Institute of Montpellier
9 IPSIM - Institut des Sciences des Plantes de Montpellier
Hélène Déméné
- Fonction : Auteur
- PersonId : 738945
- IdHAL : helene-demene
- ORCID : 0000-0002-7531-4309
Florence Vignols
Connectez-vous pour contacter l'auteur
- Fonction : Auteur correspondant
- PersonId : 180493
- IdHAL : florence-vignols
- ORCID : 0000-0002-2031-0407
- IdRef : 150001894
Connectez-vous pour contacter l'auteur
Résumé
Viruses of the sobemovirus genus are plant viruses, most of which generate very important agricultural and financial losses. Among them, the rice yellow mottle virus (RYMV) is one of the most damaging pathogens devastating rice fields in Africa. RYMV infectivity and propagation rely on its protein P1, identified as a key movement and potential long-distance RNA silencing suppressor. Here we describe P1′s complete 3D structure and dynamics obtained by an integrative approach combining X-Ray crystallography and NMR spectroscopy. We show that P1 is organized in two semi-independent and topologically unrelated domains, each harboring an original zinc finger. The two domains exhibit different affinities for zinc and sensitivities to oxidoreduction conditions, making the C-terminal P1 region a potential labile sensor of the plant redox status. An additional level of regulation resides on the capacity of P1 to oligomerize through its N-terminal domain. Coupling P1 structure information with site-directed mutagenesis and plant functional assays, we identified key residues in each zinc domain essential for infectivity and spread in rice tissues. Altogether, our results provide the first complete structure of a sobemoviral P1 movement protein and highlight structural and dynamical properties that may serve RYMV functions to infect and invade its host plant.
Format du dépôt | Fichier |
---|---|
Type de dépôt | Article dans une revue |
Titre |
en
A Flexible and Original Architecture of Two Unrelated Zinc Fingers Underlies the Role of the Multitask P1 in RYMV Spread
|
Résumé |
en
Viruses of the sobemovirus genus are plant viruses, most of which generate very important agricultural and financial losses. Among them, the rice yellow mottle virus (RYMV) is one of the most damaging pathogens devastating rice fields in Africa. RYMV infectivity and propagation rely on its protein P1, identified as a key movement and potential long-distance RNA silencing suppressor. Here we describe P1′s complete 3D structure and dynamics obtained by an integrative approach combining X-Ray crystallography and NMR spectroscopy. We show that P1 is organized in two semi-independent and topologically unrelated domains, each harboring an original zinc finger. The two domains exhibit different affinities for zinc and sensitivities to oxidoreduction conditions, making the C-terminal P1 region a potential labile sensor of the plant redox status. An additional level of regulation resides on the capacity of P1 to oligomerize through its N-terminal domain. Coupling P1 structure information with site-directed mutagenesis and plant functional assays, we identified key residues in each zinc domain essential for infectivity and spread in rice tissues. Altogether, our results provide the first complete structure of a sobemoviral P1 movement protein and highlight structural and dynamical properties that may serve RYMV functions to infect and invade its host plant.
|
Auteur(s) |
Vianney Poignavent
1
, François Hoh
2, 3
, Guillaume Terral
4
, Yinshan Yang
2, 3
, François-Xavier Gillet
5
, Jeong-Hyeon Kim
6
, Frédéric Allemand
2, 3
, Eric Lacombe
7
, Christophe Brugidou
8
, Sarah Cianferani
4
, Hélène Déméné
2, 3
, Florence Vignols
9
1
IBMP -
Institut de Biologie Moléculaire des Plantes
( 444 )
- IBMP - CNRS 12 Rue du général Zimmer 67084 STRASBOURG CEDEX
- France
2
CBS -
Centre de Biologie Structurale [Montpellier]
( 1100674 )
- 29 rue de Navacelles 34090 Montpellier Cedex
- France
3
BCM -
BioCampus
( 1100838 )
- 141, rue de la cardonille 34094 Montpellier Cedex 05
- France
4
LSMBO -
Laboratoire de Spectrométrie de Masse BioOrganique [Strasbourg]
( 550067 )
- 23 rue du loess - BP28,
67037 Strasbourg cedex 2
- France
5
MAP -
Microbiologie, adaptation et pathogénie
( 24483 )
- Bât André Lwoff, 10 rue Dubois Domaine Scientifique de la Doua 69622 VILLEURBANNE CEDEX
- France
6
UMR IPME -
UMR - Interactions Plantes Microorganismes Environnement
( 421268 )
- IRD France-Sud 911, avenue Agropolis BP 64501 34394 Montpellier cedex 5
- France
7
UMR DIADE -
Diversité, adaptation, développement des plantes
( 1100723 )
- Centre IRD de Montpellier 911 av Agropolis BP 604501 34394 Montpellier cedex 5
- France
8
UMR PHIM -
Plant Health Institute of Montpellier
( 1100829 )
- CIRAD Campus International de Baillarguet TA A-54/K
34398 Montpellier
- France
9
IPSIM -
Institut des Sciences des Plantes de Montpellier
( 1100824 )
- Bât. 7 - 2 place Pierre Viala - 34060 Montpellier cedex 2
- France
|
Licence |
Paternité
|
Langue du document |
Anglais
|
Nom de la revue |
|
Vulgarisation |
Non
|
Comité de lecture |
Oui
|
Audience |
Internationale
|
Volume |
434
|
Numéro |
16
|
Page/Identifiant |
167715
|
Public visé |
Scientifique
|
Date de publication |
2022
|
Date de publication électronique |
2022-07-04
|
Domaine(s) |
|
Projet(s) ANR |
|
Financement |
|
DOI | 10.1016/j.jmb.2022.167715 |
Base Horizon | fdi:010085889 |
UT key WOS | 000831709200004 |
Fichier principal
Poignavent et al 2022 P1rymv structure-function in JMB.pdf ( 2.79 Mo
)
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