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Article: In silico analysis of acyl-CoA-binding protein expression in soybean

TitleIn silico analysis of acyl-CoA-binding protein expression in soybean
Authors
KeywordsAbiotic stress
Acyl-CoA-binding protein
Biotic stress
Glycine max
Lipid trafficking
Microarray
Transcriptomics
Protein structure
Issue Date2021
PublisherFrontiers Research Foundation. The Journal's web site is located at http://www.frontiersin.org/plant_science/
Citation
Frontiers in Plant Science, 2021, v. 12, article no. 646938 How to Cite?
AbstractPlant 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.
Persistent Identifierhttp://hdl.handle.net/10722/299092
ISSN
2023 Impact Factor: 4.1
2023 SCImago Journal Rankings: 1.023
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorAzlan, NS-
dc.contributor.authorGuo, ZH-
dc.contributor.authorYung, WS-
dc.contributor.authorWang, Z-
dc.contributor.authorLam, HM-
dc.contributor.authorLung, SC-
dc.contributor.authorChye, ML-
dc.date.accessioned2021-04-28T02:26:04Z-
dc.date.available2021-04-28T02:26:04Z-
dc.date.issued2021-
dc.identifier.citationFrontiers in Plant Science, 2021, v. 12, article no. 646938-
dc.identifier.issn1664-462X-
dc.identifier.urihttp://hdl.handle.net/10722/299092-
dc.description.abstractPlant 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.-
dc.languageeng-
dc.publisherFrontiers Research Foundation. The Journal's web site is located at http://www.frontiersin.org/plant_science/-
dc.relation.ispartofFrontiers in Plant Science-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectAbiotic stress-
dc.subjectAcyl-CoA-binding protein-
dc.subjectBiotic stress-
dc.subjectGlycine max-
dc.subjectLipid trafficking-
dc.subjectMicroarray-
dc.subjectTranscriptomics-
dc.subjectProtein structure-
dc.titleIn silico analysis of acyl-CoA-binding protein expression in soybean-
dc.typeArticle-
dc.identifier.emailGuo, ZH: zhguo1990@hku.hk-
dc.identifier.emailLung, SC: sclung@hku.hk-
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hk-
dc.identifier.authorityChye, ML=rp00687-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.3389/fpls.2021.646938-
dc.identifier.pmid33936134-
dc.identifier.pmcidPMC8082252-
dc.identifier.scopuseid_2-s2.0-85104968106-
dc.identifier.hkuros322315-
dc.identifier.volume12-
dc.identifier.spagearticle no. 646938-
dc.identifier.epagearticle no. 646938-
dc.identifier.isiWOS:000645127100001-
dc.publisher.placeSwitzerland-

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