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...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2020-03-01
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| Series: | FEBS Open Bio |
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| Online Access: | https://doi.org/10.1002/2211-5463.12804 |
| _version_ | 1818342560177848320 |
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| author | Guanting Niu Zhuqing Shao Chuanfa Liu Tianshu Chen Qingsong Jiao Zhi Hong |
| author_facet | Guanting Niu Zhuqing Shao Chuanfa Liu Tianshu Chen Qingsong Jiao Zhi Hong |
| author_sort | Guanting Niu |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-13T16:16:38Z |
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| id | doaj.art-8cb880add93a4c7da897b494d0a9158d |
| institution | Directory Open Access Journal |
| issn | 2211-5463 |
| language | English |
| last_indexed | 2024-12-13T16:16:38Z |
| publishDate | 2020-03-01 |
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| spelling | doaj.art-8cb880add93a4c7da897b494d0a9158d2022-12-21T23:38:50ZengWileyFEBS Open Bio2211-54632020-03-0110346848310.1002/2211-5463.12804Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoformsGuanting Niu0Zhuqing Shao1Chuanfa Liu2Tianshu Chen3Qingsong Jiao4Zhi Hong5State Key Laboratory of Pharmaceutical Biotechnology NJU Advanced Institute for Life Sciences (NAILS) School of Life Sciences Nanjing University ChinaState Key Laboratory of Pharmaceutical Biotechnology NJU Advanced Institute for Life Sciences (NAILS) School of Life Sciences Nanjing University ChinaDepartment of Biology Institute of Plant and Food Science Southern University of Science and Technology Shenzhen ChinaState Key Laboratory of Pharmaceutical Biotechnology NJU Advanced Institute for Life Sciences (NAILS) School of Life Sciences Nanjing University ChinaState Key Laboratory of Pharmaceutical Biotechnology NJU Advanced Institute for Life Sciences (NAILS) School of Life Sciences Nanjing University ChinaState Key Laboratory of Pharmaceutical Biotechnology NJU Advanced Institute for Life Sciences (NAILS) School of Life Sciences Nanjing University ChinaSTT3 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.https://doi.org/10.1002/2211-5463.12804evolutionN‐glycosylationoligosaccharyltransferaseselection pressuresubunit cooperation |
| spellingShingle | Guanting Niu Zhuqing Shao Chuanfa Liu Tianshu Chen Qingsong Jiao Zhi Hong Comparative and evolutionary analyses of the divergence of plant oligosaccharyltransferase STT3 isoforms FEBS Open Bio evolution N‐glycosylation oligosaccharyltransferase selection pressure subunit cooperation |
| 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 | evolution N‐glycosylation oligosaccharyltransferase selection pressure subunit cooperation |
| url | https://doi.org/10.1002/2211-5463.12804 |
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