Nucleotide sequence of the gene from the cyanobacterium Anacystis nidulans R2 encoding the Mn-stabilizing protein involved in photosystem II water oxidation.
Nucleotide sequence of the gene from the cyanobacterium Anacystis nidulans R2 encoding the Mn-stabilizing protein involved in photosystem II water oxidation.
复制标题
来自蓝藻 Anacystis nidulans R2 的基因的核苷酸序列，编码参与光系统 II 水氧化的 Mn 稳定蛋白。
DOI：
10.1073/pnas.84.23.8230
复制
发表时间：
1987
影响因子：
11.1
通讯作者：
Sherman,LA
中科院分区：
文献类型：
--
作者：
Kuwabara,T;Reddy,KJ;Sherman,LA
从蓝藻 Anacystis nidulans R2 的基因组中克隆并测序了参与光系统 II 水氧化的 Mn 稳定蛋白（MSP；所谓的外源 33-kDa 蛋白）基因。该基因（此处指定为 woxA）被证明以单个拷贝的形式存在。推导的氨基酸序列表明翻译产物由277个氨基酸残基组成，Mr为29,306。将该序列与菠菜叶绿体成熟MSP的序列进行比较表明，翻译产物是前体，其氨基末端28个氨基酸残基代表蛋白质穿过类囊体膜进入管腔的信号肽。推定信号肽的长度小于高等植物类囊体腔蛋白转运肽的一半，而推定信号肽的结构特征与高等植物转运肽的羧基末端部分相似。成熟A. nidulans R2 MSP的氨基酸序列与高等植物MSP的同源性相当低(48-49%)，但保守的氨基酸残基似乎聚集在一起。初步分配了五个簇，其中同源性值在66-70%的范围内。对于 MSP 功能至关重要的域预计位于这些集群中。值得注意的是，MSP中的两个半胱氨酸残基是保守的，它们之间的二硫键可能在维持MSP的三级结构中发挥重要作用。
The gene for the Mn-stabilizing protein (MSP; the so-called extrinsic 33-kDa protein) that is involved in photosystem II water oxidation was cloned and sequenced from the genome of the cyanobacterium Anacystis nidulans R2. The gene (here designated woxA) was shown to be present in a single copy. The deduced amino acid sequence indicated that the translation product consisted of 277 amino acid residues with a Mr of 29,306. The comparison of the sequence with that of mature MSP from spinach chloroplasts suggested that the translation product is a precursor whose amino-terminal 28 amino acid residues represent the signal peptide for the protein to cross the thylakoid membrane into the lumen. The length of the putative signal peptide was less than half that of the transit peptide for thylakoid-lumenal proteins of higher plants, whereas the structural profile of the putative signal peptide was similar to that of the carboxyl-terminal portion of the higher plant transit peptides. The amino acid sequence of the mature A. nidulans R2 MSP showed rather low homology (48-49%) to higher plant MSPs, but the conserved amino acid residues appeared to be clustered. Five clusters were tentatively assigned, in which the homology values were in a range of 66-70%. Domains essential for the functioning of MSP are expected to be situated in these clusters. It is of note that the two cysteine residues in MSP were conserved, and the disulfide linkage between them may play an important role in maintaining the tertiary structure of MSP.