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不同光照强度下培养的隐藻绿藻珠蛋白天线的蛋白质组分析。

Proteomic analysis of the phycobiliprotein antenna of the cryptophyte alga Guillardia theta cultured under different light intensities.

机构信息

Department of Chemistry, Umeå University, 90187, Umeå, Sweden.

Botany Department, University of British Columbia, Vancouver, BC, V6T 1Z4, Canada.

出版信息

Photosynth Res. 2018 Mar;135(1-3):149-163. doi: 10.1007/s11120-017-0400-0. Epub 2017 May 24.

DOI:10.1007/s11120-017-0400-0
PMID:28540588
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5784005/
Abstract

Plants and algae have developed various light-harvesting mechanisms for optimal delivery of excitation energy to the photosystems. Cryptophyte algae have evolved a novel soluble light-harvesting antenna utilizing phycobilin pigments to complement the membrane-intrinsic Chl a/c-binding LHC antenna. This new antenna consists of the plastid-encoded β-subunit, a relic of the ancestral phycobilisome, and a novel nuclear-encoded α-subunit unique to cryptophytes. Together, these proteins form the active αβ·αβ-tetramer. In all cryptophyte algae investigated so far, the α-subunits have duplicated and diversified into a large gene family. Although there is transcriptional evidence for expression of all these genes, the X-ray structures determined to date suggest that only two of the α-subunit genes might be significantly expressed at the protein level. Using proteomics, we show that in phycoerythrin 545 (PE545) of Guillardia theta, the only cryptophyte with a sequenced genome, all 20 α-subunits are expressed when the algae grow under white light. The expression level of each protein depends on the intensity of the growth light, but there is no evidence for a specific light-dependent regulation of individual members of the α-subunit family under the growth conditions applied. GtcpeA10 seems to be a special member of the α-subunit family, because it consists of two similar N- and C-terminal domains, which likely are the result of a partial tandem gene duplication. The proteomics data of this study have been deposited to the ProteomeXchange Consortium and have the dataset identifiers PXD006301 and 10.6019/PXD006301.

摘要

植物和藻类已经发展出各种不同的光捕获机制,以将激发能最佳地传递到光系统。隐藻已经进化出一种利用藻胆体色素来补充膜内在的 Chl a/c 结合 LHC 天线的新型可溶性光捕获天线。这种新天线由质体编码的β亚基组成,这是祖先藻胆体的遗迹,以及一种独特的核编码的α亚基,这是隐藻所特有的。这两种蛋白共同构成了活性的αβ·αβ四聚体。在迄今为止研究的所有隐藻中,α亚基已经发生了复制和多样化,形成了一个庞大的基因家族。尽管有转录证据表明所有这些基因都有表达,但到目前为止确定的 X 射线结构表明,只有两个α亚基基因可能在蛋白质水平上得到显著表达。通过蛋白质组学,我们发现在具有测序基因组的隐藻中,当藻类在白光下生长时,PE545(PE545)中的所有 20 个α亚基都有表达。每种蛋白质的表达水平都取决于生长光的强度,但在应用的生长条件下,没有证据表明α亚基家族的各个成员存在特定的光依赖性调节。GtcpeA10 似乎是α亚基家族的一个特殊成员,因为它由两个相似的 N-和 C-末端结构域组成,这可能是部分串联基因复制的结果。本研究的蛋白质组学数据已被提交给 ProteomeXchange 联盟,并具有数据集标识符 PXD006301 和 10.6019/PXD006301。

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本文引用的文献

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