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在乌拉尔图小麦中克隆和鉴定的两个质体1中新型囊泡诱导蛋白基因。

Two Novel Vesicle-Inducing Proteins in Plastids 1 Genes Cloned and Characterized in Triticum urartu.

作者信息

Gao Fei, Chen Bo, Jiao Juan, Jia Lijia, Liu Cuimin

机构信息

State Key Laboratory of Plant Cell and Chromosome Engineering, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.

Department of Clinical Laboratory, PLA Army General Hospital, Beijing, PR China.

出版信息

PLoS One. 2017 Jan 19;12(1):e0170439. doi: 10.1371/journal.pone.0170439. eCollection 2017.

DOI:10.1371/journal.pone.0170439
PMID:28103282
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5245824/
Abstract

Vesicle-inducing protein in plastids 1 (Vipp1) is thought to play an important role both in thylakoid biogenesis and chloroplast envelope maintenance during stress. Vipp1 is conserved in photosynthetic organisms and forms a high homo-oligomer complex structure that may help sustain the membrane integrity of chloroplasts. This study cloned two novel VIPP1 genes from Triticum urartu and named them TuVipp1 and TuVipp2. Both proteins shared high identity with the homologous proteins AtVipp1 and CrVipp1. TuVipp1 and TuVipp2 were expressed in various organs of common wheat, and both genes were induced by light and various stress treatments. Purified TuVipp1 and TuVipp2 proteins showed secondary and advanced structures similar to those of the homologous proteins. Similar to AtVipp1, TuVipp1 is a chloroplast target protein. Additionally, TuVipp1 was able to rescue the phenotypes of pale leaves, lethality, and disordered chloroplast structures of AtVipp1 (-/-) mutant lines. Collectively, our data demonstrate that TuVipp1 and TuVipp2 are functional proteins in chloroplasts in wheat and may be critical for maintaining the chloroplast envelope under stress and membrane biogenesis upon photosynthesis.

摘要

质体中诱导囊泡蛋白1(Vipp1)被认为在应激期间的类囊体生物发生和叶绿体包膜维持中都发挥着重要作用。Vipp1在光合生物中保守,并形成一种高度同源寡聚体复合物结构,这可能有助于维持叶绿体的膜完整性。本研究从小麦野生二粒小麦中克隆了两个新的VIPP1基因,并将它们命名为TuVipp1和TuVipp2。这两种蛋白质与同源蛋白AtVipp1和CrVipp1具有高度同源性。TuVipp1和TuVipp2在普通小麦的各个器官中表达,并且这两个基因都受到光和各种应激处理的诱导。纯化的TuVipp1和TuVipp2蛋白显示出与同源蛋白相似的二级和高级结构。与AtVipp1相似,TuVipp1是一种叶绿体靶向蛋白。此外,TuVipp1能够挽救AtVipp1(-/-)突变株系的叶片苍白、致死性和叶绿体结构紊乱的表型。总体而言,我们的数据表明TuVipp1和TuVipp2是小麦叶绿体中的功能蛋白,并且可能对于在应激下维持叶绿体包膜以及光合作用时的膜生物发生至关重要。

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本文引用的文献

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Plant Physiol. 2016 Jul;171(3):1983-95. doi: 10.1104/pp.16.00532. Epub 2016 May 12.
2
α-Helical Domains Affecting the Oligomerization of Vipp1 and Its Interaction with Hsp70/DnaK in Chlamydomonas.影响衣藻中Vipp1寡聚化及其与Hsp70/DnaK相互作用的α-螺旋结构域
Biochemistry. 2015 Aug 11;54(31):4877-89. doi: 10.1021/acs.biochem.5b00050. Epub 2015 Jul 30.
3
The effect of the dark interval in intermittent light on thylakoid development: photosynthetic unit formation and light harvesting protein accumulation.
番茄基因通过叶绿体类囊体膜的正常发育对植物生存至关重要。
Front Plant Sci. 2020 Aug 26;11:1305. doi: 10.3389/fpls.2020.01305. eCollection 2020.
4
Functional Implications of Multiple IM30 Oligomeric States.多种IM30寡聚状态的功能意义
Front Plant Sci. 2019 Nov 21;10:1500. doi: 10.3389/fpls.2019.01500. eCollection 2019.
黑暗间隔对间歇光中类囊体发育的影响:光合单位的形成和光捕获蛋白的积累。
Photosynth Res. 1987 Jan;14(3):241-58. doi: 10.1007/BF00032708.
4
Draft genome of the wheat A-genome progenitor Triticum urartu.小麦 A 基因组祖先乌拉尔图小麦的草图基因组。
Nature. 2013 Apr 4;496(7443):87-90. doi: 10.1038/nature11997. Epub 2013 Mar 24.
5
The first α-helical domain of the vesicle-inducing protein in plastids 1 promotes oligomerization and lipid binding.质体 1 囊泡诱导蛋白的第一个 α-螺旋结构域促进寡聚化和脂质结合。
Planta. 2013 Feb;237(2):529-40. doi: 10.1007/s00425-012-1772-1. Epub 2012 Oct 2.
6
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