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Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA

Protein modification by the small ubiquitin-like modifier (SUMO) plays an important role in multiple plant processes, including growth, development, and the response to abiotic stresses. Mechanistically, SUMOylation is a sequential multi-enzymatic process where SUMO E3 ligases accelerate SUMO conjug...

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Detalles Bibliográficos
Autores principales: Jmii, Souleimen, Cappadocia, Laurent
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8064691/
https://www.ncbi.nlm.nih.gov/pubmed/33897743
http://dx.doi.org/10.3389/fpls.2021.652170
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author Jmii, Souleimen
Cappadocia, Laurent
author_facet Jmii, Souleimen
Cappadocia, Laurent
author_sort Jmii, Souleimen
collection PubMed
description Protein modification by the small ubiquitin-like modifier (SUMO) plays an important role in multiple plant processes, including growth, development, and the response to abiotic stresses. Mechanistically, SUMOylation is a sequential multi-enzymatic process where SUMO E3 ligases accelerate SUMO conjugation while also influencing target identity and interactions. This review explores the biological functions of plant SUMO E3 ligases [SAP AND MIZ1 DOMAIN-CONTAINING LIGASE (SIZs), METHYL METHANESULFONATE-SENSITIVITY PROTEIN 21 (MMS21s), and PROTEIN INHIBITOR OF ACTIVATED STAT-LIKE (PIALs)] in relation to their molecular activities and domains. We also explore the sub-cellular localization of SUMO E3 ligases and review evidence suggesting a connection between certain SUMO E3 ligases and DNA that contributes to gene expression regulation.
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spelling pubmed-80646912021-04-24 Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA Jmii, Souleimen Cappadocia, Laurent Front Plant Sci Plant Science Protein modification by the small ubiquitin-like modifier (SUMO) plays an important role in multiple plant processes, including growth, development, and the response to abiotic stresses. Mechanistically, SUMOylation is a sequential multi-enzymatic process where SUMO E3 ligases accelerate SUMO conjugation while also influencing target identity and interactions. This review explores the biological functions of plant SUMO E3 ligases [SAP AND MIZ1 DOMAIN-CONTAINING LIGASE (SIZs), METHYL METHANESULFONATE-SENSITIVITY PROTEIN 21 (MMS21s), and PROTEIN INHIBITOR OF ACTIVATED STAT-LIKE (PIALs)] in relation to their molecular activities and domains. We also explore the sub-cellular localization of SUMO E3 ligases and review evidence suggesting a connection between certain SUMO E3 ligases and DNA that contributes to gene expression regulation. Frontiers Media S.A. 2021-04-09 /pmc/articles/PMC8064691/ /pubmed/33897743 http://dx.doi.org/10.3389/fpls.2021.652170 Text en Copyright © 2021 Jmii and Cappadocia. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Jmii, Souleimen
Cappadocia, Laurent
Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA
title Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA
title_full Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA
title_fullStr Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA
title_full_unstemmed Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA
title_short Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA
title_sort plant sumo e3 ligases: function, structural organization, and connection with dna
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8064691/
https://www.ncbi.nlm.nih.gov/pubmed/33897743
http://dx.doi.org/10.3389/fpls.2021.652170
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