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硅藻的捕光蛋白:它们与高等植物叶绿素a/b结合蛋白的关系及其向质体的转运模式。

Light-harvesting proteins of diatoms: their relationship to the chlorophyll a/b binding proteins of higher plants and their mode of transport into plastids.

作者信息

Grossman A, Manodori A, Snyder D

机构信息

Carnegie Institute of Washington, Stanford, CA 94305.

出版信息

Mol Gen Genet. 1990 Oct;224(1):91-100. doi: 10.1007/BF00259455.

Abstract

We have cloned and characterized members of a gene family encoding polypeptide constituents of the fucoxanthin, chlorophyll a/c protein complex, a light-harvesting complex associated with photosystem II of diatoms and brown algae. Three cDNA clones encoding proteins associated with this complex in the diatom Phaeodactylum tricornutum have been isolated. As deduced from the nucleotide sequences, these light-harvesting proteins show homology to the chlorophyll a/b binding polypeptides of higher plants. Specifically, the N-terminal regions of the fucoxanthin, chlorophyll a/c-binding proteins are homologous to the chlorophyll a/b binding proteins in both the third membrane-spanning domain and the stroma-exposed region between membrane-spanning domains 2 and 3. Like the chlorophyll a/b-binding proteins, the mature fucoxanthin, chlorophyll a/c polypeptides have three hydrophobic alpha-helical domains which could span the membrane bilayer. The similarities between the two light-harvesting proteins might reflect the fact that both bind chlorophyll molecules and/or might be important for maintaining certain structural features of the complex. There is little similarity between the N-terminal sequences of the primary translation products of the fucoxanthin, chlorophyll a/c proteins and any transit sequences that have been characterized. Instead, the N-terminal sequences have features resembling those of signal sequences. Thus either transit peptides used in P. tricornutum show little resemblance to those of higher plants and green algae or the nuclear-encoded plastid proteins enter the organelle via a mechanism different from that used in higher plants.

摘要

我们克隆并鉴定了一个基因家族的成员,该家族编码岩藻黄质叶绿素a/c蛋白复合体的多肽成分,这是一种与硅藻和褐藻光系统II相关的捕光复合体。已从硅藻三角褐指藻中分离出三个编码与该复合体相关蛋白质的cDNA克隆。根据核苷酸序列推断,这些捕光蛋白与高等植物的叶绿素a/b结合多肽具有同源性。具体而言,岩藻黄质叶绿素a/c结合蛋白的N端区域在第三个跨膜结构域以及跨膜结构域2和3之间的基质暴露区域与叶绿素a/b结合蛋白同源。与叶绿素a/b结合蛋白一样,成熟的岩藻黄质叶绿素a/c多肽具有三个可跨越膜双层的疏水α螺旋结构域。这两种捕光蛋白之间的相似性可能反映了它们都结合叶绿素分子这一事实,和/或可能对维持复合体的某些结构特征很重要。岩藻黄质叶绿素a/c蛋白初级翻译产物的N端序列与任何已鉴定的转运序列几乎没有相似性。相反,N端序列具有类似于信号序列的特征。因此,要么三角褐指藻中使用的转运肽与高等植物和绿藻的转运肽几乎没有相似性,要么核编码的质体蛋白通过一种不同于高等植物的机制进入细胞器。

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