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Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoforms

STT3 is a catalytic subunit of hetero‐oligomeric oligosaccharyltransferase (OST), which is important for asparagine‐linked glycosylation. In mammals and plants, OSTs with different STT3 isoforms exhibit distinct levels of enzymatic efficiency or different responses to stressors. Although two differe...

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Autores principales: Niu, Guanting, Shao, Zhuqing, Liu, Chuanfa, Chen, Tianshu, Jiao, Qingsong, Hong, Zhi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7050244/
https://www.ncbi.nlm.nih.gov/pubmed/32011067
http://dx.doi.org/10.1002/2211-5463.12804
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author Niu, Guanting
Shao, Zhuqing
Liu, Chuanfa
Chen, Tianshu
Jiao, Qingsong
Hong, Zhi
author_facet Niu, Guanting
Shao, Zhuqing
Liu, Chuanfa
Chen, Tianshu
Jiao, Qingsong
Hong, Zhi
author_sort Niu, Guanting
collection PubMed
description STT3 is a catalytic subunit of hetero‐oligomeric oligosaccharyltransferase (OST), which is important for asparagine‐linked glycosylation. In mammals and plants, OSTs with different STT3 isoforms exhibit distinct levels of enzymatic efficiency or different responses to stressors. Although two different STT3 isoforms have been identified in both plants and animals, it remains unclear whether these isoforms result from gene duplication in an ancestral eukaryote. Furthermore, the molecular mechanisms underlying the functional divergences between the two STT3 isoforms in plant have not been well elucidated. Here, we conducted phylogenetic analysis of the major evolutionary node species and suggested that gene duplications of STT3 may have occurred independently in animals and plants. Across land plants, the exon–intron structure differed between the two STT3 isoforms, but was highly conserved for each isoform. Most angiosperm STT3a genes had 23 exons with intron phase 0, while STT3b genes had 6 exons with intron phase 2. Characteristic motifs (motif 18 and 19) of STT3s were mapped to different structure domains in the plant STT3 proteins. These two motifs overlap with regions of high nonsynonymous‐to‐synonymous substitution rates, suggesting the regions may be related to functional difference between STT3a and STT3b. In addition, promoter elements and gene expression profiles were different between the two isoforms, indicating expression pattern divergence of the two genes. Collectively, the identified differences may result in the functional divergence of plant STT3s.
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spelling pubmed-70502442020-03-05 Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoforms Niu, Guanting Shao, Zhuqing Liu, Chuanfa Chen, Tianshu Jiao, Qingsong Hong, Zhi FEBS Open Bio Research Articles STT3 is a catalytic subunit of hetero‐oligomeric oligosaccharyltransferase (OST), which is important for asparagine‐linked glycosylation. In mammals and plants, OSTs with different STT3 isoforms exhibit distinct levels of enzymatic efficiency or different responses to stressors. Although two different STT3 isoforms have been identified in both plants and animals, it remains unclear whether these isoforms result from gene duplication in an ancestral eukaryote. Furthermore, the molecular mechanisms underlying the functional divergences between the two STT3 isoforms in plant have not been well elucidated. Here, we conducted phylogenetic analysis of the major evolutionary node species and suggested that gene duplications of STT3 may have occurred independently in animals and plants. Across land plants, the exon–intron structure differed between the two STT3 isoforms, but was highly conserved for each isoform. Most angiosperm STT3a genes had 23 exons with intron phase 0, while STT3b genes had 6 exons with intron phase 2. Characteristic motifs (motif 18 and 19) of STT3s were mapped to different structure domains in the plant STT3 proteins. These two motifs overlap with regions of high nonsynonymous‐to‐synonymous substitution rates, suggesting the regions may be related to functional difference between STT3a and STT3b. In addition, promoter elements and gene expression profiles were different between the two isoforms, indicating expression pattern divergence of the two genes. Collectively, the identified differences may result in the functional divergence of plant STT3s. John Wiley and Sons Inc. 2020-02-19 /pmc/articles/PMC7050244/ /pubmed/32011067 http://dx.doi.org/10.1002/2211-5463.12804 Text en © 2020 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Niu, Guanting
Shao, Zhuqing
Liu, Chuanfa
Chen, Tianshu
Jiao, Qingsong
Hong, Zhi
Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoforms
title Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoforms
title_full Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoforms
title_fullStr Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoforms
title_full_unstemmed Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoforms
title_short Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoforms
title_sort comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase stt3 isoforms
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7050244/
https://www.ncbi.nlm.nih.gov/pubmed/32011067
http://dx.doi.org/10.1002/2211-5463.12804
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