Literature DB >> 22988854

LEA proteins: IDPs with versatile functions in cellular dehydration tolerance.

Dirk K Hincha1, Anja Thalhammer.   

Abstract

LEA (late embryogenesis abundant) proteins were originally described almost 30 years ago as accumulating late in plant seed development. They were later found to be induced in vegetative plant tissues under environmental stress conditions and also in desiccation-tolerant micro-organisms and invertebrates. Although they are widely assumed to play crucial roles in cellular dehydration tolerance, their physiological and biochemical functions are largely unknown. Most LEA proteins are predicted to be intrinsically disordered and this has been experimentally verified in several cases. In addition, some LEA proteins partially fold, mainly into α-helices, during drying or in the presence of membranes. Recent studies have concentrated on the potential roles of LEA proteins in stabilizing membranes or sensitive enzymes during freezing or drying, and the present review concentrates on these two possible functions of LEA proteins in cellular dehydration tolerance.

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Year:  2012        PMID: 22988854     DOI: 10.1042/BST20120109

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN: 0300-5127            Impact factor:   5.407


  61 in total

1.  Protecting activity of desiccated enzymes.

Authors:  Samantha Piszkiewicz; Kathryn H Gunn; Owen Warmuth; Ashlee Propst; Aakash Mehta; Kenny H Nguyen; Elizabeth Kuhlman; Alex J Guseman; Samantha S Stadmiller; Thomas C Boothby; Saskia B Neher; Gary J Pielak
Journal:  Protein Sci       Date:  2019-03-30       Impact factor: 6.725

2.  Structural properties and cellular expression of AfrLEA6, a group 6 late embryogenesis abundant protein from embryos of Artemia franciscana.

Authors:  Blase M LeBlanc; Mike T Le; Brett Janis; Michael A Menze; Steven C Hand
Journal:  Cell Stress Chaperones       Date:  2019-07-30       Impact factor: 3.667

Review 3.  Structural disorder in plant proteins: where plasticity meets sessility.

Authors:  Alejandra A Covarrubias; Cesar L Cuevas-Velazquez; Paulette S Romero-Pérez; David F Rendón-Luna; Caspar C C Chater
Journal:  Cell Mol Life Sci       Date:  2017-06-22       Impact factor: 9.261

4.  Effect of an Intrinsically Disordered Plant Stress Protein on the Properties of Water.

Authors:  Luisa A Ferreira; Alicyia Walczyk Mooradally; Boris Zaslavsky; Vladimir N Uversky; Steffen P Graether
Journal:  Biophys J       Date:  2018-09-22       Impact factor: 4.033

5.  Folding and Lipid Composition Determine Membrane Interaction of the Disordered Protein COR15A.

Authors:  Carlos Navarro-Retamal; Anne Bremer; Helgi I Ingólfsson; Jans Alzate-Morales; Julio Caballero; Anja Thalhammer; Wendy González; Dirk K Hincha
Journal:  Biophys J       Date:  2018-08-18       Impact factor: 4.033

6.  Functional characterization of selected LEA proteins from Arabidopsis thaliana in yeast and in vitro.

Authors:  Nghiem X Dang; Antoneta V Popova; Michaela Hundertmark; Dirk K Hincha
Journal:  Planta       Date:  2014-05-20       Impact factor: 4.116

7.  Group 1 LEA proteins contribute to the desiccation and freeze tolerance of Artemia franciscana embryos during diapause.

Authors:  Jantina Toxopeus; Alden H Warner; Thomas H MacRae
Journal:  Cell Stress Chaperones       Date:  2014-05-21       Impact factor: 3.667

8.  A group 6 late embryogenesis abundant protein from common bean is a disordered protein with extended helical structure and oligomer-forming properties.

Authors:  Lucero Y Rivera-Najera; Gloria Saab-Rincón; Marina Battaglia; Carlos Amero; Nancy O Pulido; Enrique García-Hernández; Rosa M Solórzano; José L Reyes; Alejandra A Covarrubias
Journal:  J Biol Chem       Date:  2014-09-30       Impact factor: 5.157

9.  Disordered cold regulated15 proteins protect chloroplast membranes during freezing through binding and folding, but do not stabilize chloroplast enzymes in vivo.

Authors:  Anja Thalhammer; Gary Bryant; Ronan Sulpice; Dirk K Hincha
Journal:  Plant Physiol       Date:  2014-08-05       Impact factor: 8.340

10.  Opposing Control by Transcription Factors MYB61 and MYB3 Increases Freezing Tolerance by Relieving C-Repeat Binding Factor Suppression.

Authors:  Zhenqian Zhang; Xiaona Hu; Yunqin Zhang; Zhenyan Miao; Can Xie; Xiangzhao Meng; Jie Deng; Jiangqi Wen; Kirankumar S Mysore; Florian Frugier; Tao Wang; Jiangli Dong
Journal:  Plant Physiol       Date:  2016-08-30       Impact factor: 8.340

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