Plant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses

In response to various environmental stresses, plants have evolved a wide range of defense mechanisms, resulting in the overexpression of a series of stress-responsive genes. Among them, there is certain set of genes that encode for intrinsically disordered proteins (IDPs) that repair and protect th...

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Autores principales:	Mughair Abdul Aziz, Miloofer Sabeem, Sangeeta Kutty Mullath, Faical Brini, Khaled Masmoudi
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	abiotic stress dehydrins gene expression group II LEA protein hydrophilins Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/9f2edf6553924943b63879c7f98eba48
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spelling	oai:doaj.org-article:9f2edf6553924943b63879c7f98eba482021-11-25T16:53:30ZPlant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses10.3390/biom111116622218-273Xhttps://doaj.org/article/9f2edf6553924943b63879c7f98eba482021-11-01T00:00:00Zhttps://www.mdpi.com/2218-273X/11/11/1662https://doaj.org/toc/2218-273XIn response to various environmental stresses, plants have evolved a wide range of defense mechanisms, resulting in the overexpression of a series of stress-responsive genes. Among them, there is certain set of genes that encode for intrinsically disordered proteins (IDPs) that repair and protect the plants from damage caused by environmental stresses. Group II LEA (late embryogenesis abundant) proteins compose the most abundant and characterized group of IDPs; they accumulate in the late stages of seed development and are expressed in response to dehydration, salinity, low temperature, or abscisic acid (ABA) treatment. The physiological and biochemical characterization of group II LEA proteins has been carried out in a number of investigations because of their vital roles in protecting the integrity of biomolecules by preventing the crystallization of cellular components prior to multiple stresses. This review describes the distribution, structural architecture, and genomic diversification of group II LEA proteins, with some recent investigations on their regulation and molecular expression under various abiotic stresses. Novel aspects of group II LEA proteins in <i>Phoenix dactylifera</i> and in orthodox seeds are also presented. Genome-wide association studies (GWAS) indicated a ubiquitous distribution and expression of group II LEA genes in different plant cells. In vitro experimental evidence from biochemical assays has suggested that group II LEA proteins perform heterogenous functions in response to extreme stresses. Various investigations have indicated the participation of group II LEA proteins in the plant stress tolerance mechanism, spotlighting the molecular aspects of group II LEA genes and their potential role in biotechnological strategies to increase plants’ survival in adverse environments.Mughair Abdul AzizMiloofer SabeemSangeeta Kutty MullathFaical BriniKhaled MasmoudiMDPI AGarticleabiotic stressdehydrinsgene expressiongroup II LEA proteinhydrophilinsMicrobiologyQR1-502ENBiomolecules, Vol 11, Iss 1662, p 1662 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	abiotic stress dehydrins gene expression group II LEA protein hydrophilins Microbiology QR1-502
spellingShingle	abiotic stress dehydrins gene expression group II LEA protein hydrophilins Microbiology QR1-502 Mughair Abdul Aziz Miloofer Sabeem Sangeeta Kutty Mullath Faical Brini Khaled Masmoudi Plant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses
description	In response to various environmental stresses, plants have evolved a wide range of defense mechanisms, resulting in the overexpression of a series of stress-responsive genes. Among them, there is certain set of genes that encode for intrinsically disordered proteins (IDPs) that repair and protect the plants from damage caused by environmental stresses. Group II LEA (late embryogenesis abundant) proteins compose the most abundant and characterized group of IDPs; they accumulate in the late stages of seed development and are expressed in response to dehydration, salinity, low temperature, or abscisic acid (ABA) treatment. The physiological and biochemical characterization of group II LEA proteins has been carried out in a number of investigations because of their vital roles in protecting the integrity of biomolecules by preventing the crystallization of cellular components prior to multiple stresses. This review describes the distribution, structural architecture, and genomic diversification of group II LEA proteins, with some recent investigations on their regulation and molecular expression under various abiotic stresses. Novel aspects of group II LEA proteins in <i>Phoenix dactylifera</i> and in orthodox seeds are also presented. Genome-wide association studies (GWAS) indicated a ubiquitous distribution and expression of group II LEA genes in different plant cells. In vitro experimental evidence from biochemical assays has suggested that group II LEA proteins perform heterogenous functions in response to extreme stresses. Various investigations have indicated the participation of group II LEA proteins in the plant stress tolerance mechanism, spotlighting the molecular aspects of group II LEA genes and their potential role in biotechnological strategies to increase plants’ survival in adverse environments.
format	article
author	Mughair Abdul Aziz Miloofer Sabeem Sangeeta Kutty Mullath Faical Brini Khaled Masmoudi
author_facet	Mughair Abdul Aziz Miloofer Sabeem Sangeeta Kutty Mullath Faical Brini Khaled Masmoudi
author_sort	Mughair Abdul Aziz
title	Plant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses
title_short	Plant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses
title_full	Plant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses
title_fullStr	Plant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses
title_full_unstemmed	Plant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses
title_sort	plant group ii lea proteins: intrinsically disordered structure for multiple functions in response to environmental stresses
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/9f2edf6553924943b63879c7f98eba48
work_keys_str_mv	AT mughairabdulaziz plantgroupiileaproteinsintrinsicallydisorderedstructureformultiplefunctionsinresponsetoenvironmentalstresses AT miloofersabeem plantgroupiileaproteinsintrinsicallydisorderedstructureformultiplefunctionsinresponsetoenvironmentalstresses AT sangeetakuttymullath plantgroupiileaproteinsintrinsicallydisorderedstructureformultiplefunctionsinresponsetoenvironmentalstresses AT faicalbrini plantgroupiileaproteinsintrinsicallydisorderedstructureformultiplefunctionsinresponsetoenvironmentalstresses AT khaledmasmoudi plantgroupiileaproteinsintrinsicallydisorderedstructureformultiplefunctionsinresponsetoenvironmentalstresses
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Plant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses

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