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A Modified Actin (Gly65Val Substitution) Expressed in Cotton Disrupts Polymerization of Actin Filaments Leading to the Phenotype of Ligon Lintless-1 (Li(1)) Mutant
Dynamic remodeling of the actin cytoskeleton plays a central role in the elongation of cotton fibers, which are the most important natural fibers in the global textile industry. Here, a high-resolution mapping approach combined with comparative sequencing and a transgenic method revealed that a G65V...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7998759/ https://www.ncbi.nlm.nih.gov/pubmed/33809404 http://dx.doi.org/10.3390/ijms22063000 |
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author | Cao, Yuefen Huang, Hui Yu, Yanjun Dai, Huaqin Hao, Huanfeng Zhang, Hua Jiang, Yurong Ding, Mingquan Li, Feifei Tu, Lili Kong, Zhaosheng Rong, Junkang |
author_facet | Cao, Yuefen Huang, Hui Yu, Yanjun Dai, Huaqin Hao, Huanfeng Zhang, Hua Jiang, Yurong Ding, Mingquan Li, Feifei Tu, Lili Kong, Zhaosheng Rong, Junkang |
author_sort | Cao, Yuefen |
collection | PubMed |
description | Dynamic remodeling of the actin cytoskeleton plays a central role in the elongation of cotton fibers, which are the most important natural fibers in the global textile industry. Here, a high-resolution mapping approach combined with comparative sequencing and a transgenic method revealed that a G65V substitution in the cotton actin Gh_D04G0865 (GhACT17D in the wild-type) is responsible for the Gossypium hirsutum Ligon lintless-1 (Li(1)) mutant (GhACT17DM). In the mutant GhACT17DM from Li(1) plant, Gly65 is substituted with valine on the lip of the nucleotide-binding domain of GhACT17D, which probably affects the polymerization of F-actin. Over-expression of GhACT17DM, but not GhACT17D, driven by either a CaMV35 promoter or a fiber-specific promoter in cotton produced a Li(1)-like phenotype. Compared with the wild-type control, actin filaments in Li(1) fibers showed higher growth and shrinkage rates, decreased filament skewness and parallelness, and increased filament density. Taken together, our results indicate that the incorporation of GhACT17DM during actin polymerization disrupts the establishment and dynamics of the actin cytoskeleton, resulting in defective fiber elongation and the overall dwarf and twisted phenotype of the Li(1) mutant. |
format | Online Article Text |
id | pubmed-7998759 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-79987592021-03-28 A Modified Actin (Gly65Val Substitution) Expressed in Cotton Disrupts Polymerization of Actin Filaments Leading to the Phenotype of Ligon Lintless-1 (Li(1)) Mutant Cao, Yuefen Huang, Hui Yu, Yanjun Dai, Huaqin Hao, Huanfeng Zhang, Hua Jiang, Yurong Ding, Mingquan Li, Feifei Tu, Lili Kong, Zhaosheng Rong, Junkang Int J Mol Sci Article Dynamic remodeling of the actin cytoskeleton plays a central role in the elongation of cotton fibers, which are the most important natural fibers in the global textile industry. Here, a high-resolution mapping approach combined with comparative sequencing and a transgenic method revealed that a G65V substitution in the cotton actin Gh_D04G0865 (GhACT17D in the wild-type) is responsible for the Gossypium hirsutum Ligon lintless-1 (Li(1)) mutant (GhACT17DM). In the mutant GhACT17DM from Li(1) plant, Gly65 is substituted with valine on the lip of the nucleotide-binding domain of GhACT17D, which probably affects the polymerization of F-actin. Over-expression of GhACT17DM, but not GhACT17D, driven by either a CaMV35 promoter or a fiber-specific promoter in cotton produced a Li(1)-like phenotype. Compared with the wild-type control, actin filaments in Li(1) fibers showed higher growth and shrinkage rates, decreased filament skewness and parallelness, and increased filament density. Taken together, our results indicate that the incorporation of GhACT17DM during actin polymerization disrupts the establishment and dynamics of the actin cytoskeleton, resulting in defective fiber elongation and the overall dwarf and twisted phenotype of the Li(1) mutant. MDPI 2021-03-16 /pmc/articles/PMC7998759/ /pubmed/33809404 http://dx.doi.org/10.3390/ijms22063000 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Cao, Yuefen Huang, Hui Yu, Yanjun Dai, Huaqin Hao, Huanfeng Zhang, Hua Jiang, Yurong Ding, Mingquan Li, Feifei Tu, Lili Kong, Zhaosheng Rong, Junkang A Modified Actin (Gly65Val Substitution) Expressed in Cotton Disrupts Polymerization of Actin Filaments Leading to the Phenotype of Ligon Lintless-1 (Li(1)) Mutant |
title | A Modified Actin (Gly65Val Substitution) Expressed in Cotton Disrupts Polymerization of Actin Filaments Leading to the Phenotype of Ligon Lintless-1 (Li(1)) Mutant |
title_full | A Modified Actin (Gly65Val Substitution) Expressed in Cotton Disrupts Polymerization of Actin Filaments Leading to the Phenotype of Ligon Lintless-1 (Li(1)) Mutant |
title_fullStr | A Modified Actin (Gly65Val Substitution) Expressed in Cotton Disrupts Polymerization of Actin Filaments Leading to the Phenotype of Ligon Lintless-1 (Li(1)) Mutant |
title_full_unstemmed | A Modified Actin (Gly65Val Substitution) Expressed in Cotton Disrupts Polymerization of Actin Filaments Leading to the Phenotype of Ligon Lintless-1 (Li(1)) Mutant |
title_short | A Modified Actin (Gly65Val Substitution) Expressed in Cotton Disrupts Polymerization of Actin Filaments Leading to the Phenotype of Ligon Lintless-1 (Li(1)) Mutant |
title_sort | modified actin (gly65val substitution) expressed in cotton disrupts polymerization of actin filaments leading to the phenotype of ligon lintless-1 (li(1)) mutant |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7998759/ https://www.ncbi.nlm.nih.gov/pubmed/33809404 http://dx.doi.org/10.3390/ijms22063000 |
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