In silico Analysis of Acyl-CoA-Binding Protein Expression in Soybean
Plant acyl-CoA-binding proteins (ACBPs) form a highly conserved protein family that binds to acyl-CoA esters as well as other lipid and protein interactors to function in developmental and stress responses. This protein family had been extensively studied in non-leguminous species such as Arabidopsi...
Main Authors: | , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Frontiers Media S.A.
2021-04-01
|
Series: | Frontiers in Plant Science |
Subjects: | |
Online Access: | https://www.frontiersin.org/articles/10.3389/fpls.2021.646938/full |
_version_ | 1818429923112517632 |
---|---|
author | Nur Syifaq Azlan Ze-Hua Guo Wai-Shing Yung Zhili Wang Hon-Ming Lam Shiu-Cheung Lung Mee-Len Chye |
author_facet | Nur Syifaq Azlan Ze-Hua Guo Wai-Shing Yung Zhili Wang Hon-Ming Lam Shiu-Cheung Lung Mee-Len Chye |
author_sort | Nur Syifaq Azlan |
collection | DOAJ |
description | Plant acyl-CoA-binding proteins (ACBPs) form a highly conserved protein family that binds to acyl-CoA esters as well as other lipid and protein interactors to function in developmental and stress responses. This protein family had been extensively studied in non-leguminous species such as Arabidopsis thaliana (thale cress), Oryza sativa (rice), and Brassica napus (oilseed rape). However, the characterization of soybean (Glycine max) ACBPs, designated GmACBPs, has remained unreported although this legume is a globally important crop cultivated for its high oil and protein content, and plays a significant role in the food and chemical industries. In this study, 11 members of the GmACBP family from four classes, comprising Class I (small), Class II (ankyrin repeats), Class III (large), and Class IV (kelch motif), were identified. For each class, more than one copy occurred and their domain architecture including the acyl-CoA-binding domain was compared with Arabidopsis and rice. The expression profile, tertiary structure and subcellular localization of each GmACBP were predicted, and the similarities and differences between GmACBPs and other plant ACBPs were deduced. A potential role for some Class III GmACBPs in nodulation, not previously encountered in non-leguminous ACBPs, has emerged. Interestingly, the sole member of Class III ACBP in each of non-leguminous Arabidopsis and rice had been previously identified in plant-pathogen interactions. As plant ACBPs are known to play important roles in development and responses to abiotic and biotic stresses, the in silico expression profiles on GmACBPs, gathered from data mining of RNA-sequencing and microarray analyses, will lay the foundation for future studies in their applications in biotechnology. |
first_indexed | 2024-12-14T15:25:13Z |
format | Article |
id | doaj.art-380a2f30af1b4a10acb70155787e74f3 |
institution | Directory Open Access Journal |
issn | 1664-462X |
language | English |
last_indexed | 2024-12-14T15:25:13Z |
publishDate | 2021-04-01 |
publisher | Frontiers Media S.A. |
record_format | Article |
series | Frontiers in Plant Science |
spelling | doaj.art-380a2f30af1b4a10acb70155787e74f32022-12-21T22:56:02ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2021-04-011210.3389/fpls.2021.646938646938In silico Analysis of Acyl-CoA-Binding Protein Expression in SoybeanNur Syifaq Azlan0Ze-Hua Guo1Wai-Shing Yung2Zhili Wang3Hon-Ming Lam4Shiu-Cheung Lung5Mee-Len Chye6School of Biological Sciences, The University of Hong Kong, Pokfulam, Hong KongSchool of Biological Sciences, The University of Hong Kong, Pokfulam, Hong KongSchool of Life Sciences and Center for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, Hong KongSchool of Life Sciences and Center for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, Hong KongSchool of Life Sciences and Center for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, Hong KongSchool of Biological Sciences, The University of Hong Kong, Pokfulam, Hong KongSchool of Biological Sciences, The University of Hong Kong, Pokfulam, Hong KongPlant acyl-CoA-binding proteins (ACBPs) form a highly conserved protein family that binds to acyl-CoA esters as well as other lipid and protein interactors to function in developmental and stress responses. This protein family had been extensively studied in non-leguminous species such as Arabidopsis thaliana (thale cress), Oryza sativa (rice), and Brassica napus (oilseed rape). However, the characterization of soybean (Glycine max) ACBPs, designated GmACBPs, has remained unreported although this legume is a globally important crop cultivated for its high oil and protein content, and plays a significant role in the food and chemical industries. In this study, 11 members of the GmACBP family from four classes, comprising Class I (small), Class II (ankyrin repeats), Class III (large), and Class IV (kelch motif), were identified. For each class, more than one copy occurred and their domain architecture including the acyl-CoA-binding domain was compared with Arabidopsis and rice. The expression profile, tertiary structure and subcellular localization of each GmACBP were predicted, and the similarities and differences between GmACBPs and other plant ACBPs were deduced. A potential role for some Class III GmACBPs in nodulation, not previously encountered in non-leguminous ACBPs, has emerged. Interestingly, the sole member of Class III ACBP in each of non-leguminous Arabidopsis and rice had been previously identified in plant-pathogen interactions. As plant ACBPs are known to play important roles in development and responses to abiotic and biotic stresses, the in silico expression profiles on GmACBPs, gathered from data mining of RNA-sequencing and microarray analyses, will lay the foundation for future studies in their applications in biotechnology.https://www.frontiersin.org/articles/10.3389/fpls.2021.646938/fullabiotic stressacyl-CoA-binding proteinbiotic stressGlycine maxlipid traffickingmicroarray |
spellingShingle | Nur Syifaq Azlan Ze-Hua Guo Wai-Shing Yung Zhili Wang Hon-Ming Lam Shiu-Cheung Lung Mee-Len Chye In silico Analysis of Acyl-CoA-Binding Protein Expression in Soybean Frontiers in Plant Science abiotic stress acyl-CoA-binding protein biotic stress Glycine max lipid trafficking microarray |
title | In silico Analysis of Acyl-CoA-Binding Protein Expression in Soybean |
title_full | In silico Analysis of Acyl-CoA-Binding Protein Expression in Soybean |
title_fullStr | In silico Analysis of Acyl-CoA-Binding Protein Expression in Soybean |
title_full_unstemmed | In silico Analysis of Acyl-CoA-Binding Protein Expression in Soybean |
title_short | In silico Analysis of Acyl-CoA-Binding Protein Expression in Soybean |
title_sort | in silico analysis of acyl coa binding protein expression in soybean |
topic | abiotic stress acyl-CoA-binding protein biotic stress Glycine max lipid trafficking microarray |
url | https://www.frontiersin.org/articles/10.3389/fpls.2021.646938/full |
work_keys_str_mv | AT nursyifaqazlan insilicoanalysisofacylcoabindingproteinexpressioninsoybean AT zehuaguo insilicoanalysisofacylcoabindingproteinexpressioninsoybean AT waishingyung insilicoanalysisofacylcoabindingproteinexpressioninsoybean AT zhiliwang insilicoanalysisofacylcoabindingproteinexpressioninsoybean AT honminglam insilicoanalysisofacylcoabindingproteinexpressioninsoybean AT shiucheunglung insilicoanalysisofacylcoabindingproteinexpressioninsoybean AT meelenchye insilicoanalysisofacylcoabindingproteinexpressioninsoybean |