Rod structure of a phycoerythrin II-containing phycobilisome. I. Organization and sequence of the gene cluster encoding the major phycobiliprotein rod components in the genome of marine Synechococcus sp. WH8020.

Rod structure of a phycoerythrin II-containing phycobilisome. I. Organization and sequence of the gene cluster encoding the major phycobiliprotein rod components in the genome of marine Synechococcus sp. WH8020.
复制标题

DOI:
10.1016/s0021-9258(18)54064-3
复制
发表时间:
1993-01
期刊:
The Journal of biological chemistry
影响因子:
--
通讯作者:
S. Wilbanks;A. Glazer
S. Wilbanks;A. Glazer
中科院分区:
其他
文献类型:
--
作者:
S. Wilbanks;A. Glazer

文献摘要

被引文献

相似文献

单细胞海洋蓝细菌的藻胆体的独特之处在于具有具有两种不同藻红蛋白 PE I 和 PE II 的杆子结构,分别具有五个和六个胆素(Ong,L.J.和 Glazer,A.N.(1991)J.Biol.Chem.266, 9515-9527)。 PE I、PE II 和藻蓝蛋白的 α 和 β 亚基的基因以及 PE II 相关接头多肽的基因聚集在聚球藻基因组的单个 15 KB 区域上。 WH8020。该区域的完整测序允许明确分配这些藻胆蛋白中所有胆素附着位点的位置。其他十二个开放阅读框与上述结构基因密切相关。六个与其他蓝细菌中藻胆蛋白基因相邻的开放阅读框同源,并推断与胆素添加有关。这是所有蓝细菌中已知的此类开放阅读框数量最多的。另一个开放阅读框具有与牛蛋白磷酸酪氨酸磷酸酶的活性位点序列惊人相似的短区域。
Phycobilisomes of the unicellular marine cyanobacteria are unique in having rod substructures with two distinct phycoerythrins, PE I and PE II, with five and six bilins, respectively (Ong, L. J., and Glazer, A. N. (1991) J. Biol. Chem. 266, 9515-9527). The genes for the alpha and beta subunits of PE I, PE II, and phycocyanin, and that for the PE II-associated linker polypeptide, are clustered on a single 15-kilobase region of the genome of Synechococcus sp. WH8020. Complete sequencing of this region allowed definitive assignment of the positions of all bilin attachment sites in these phycobiliproteins. Twelve other open reading frames are closely associated with the structural genes specified above. Six are homologous to open reading frames adjacent to phycobiliprotein genes in other cyanobacteria and inferred to be involved in bilin addition. This is the largest number of open reading frames of this class known in any cyanobacterium. Another of the open reading frames has a short region of striking similarity to the active site sequence of a bovine protein-phosphotyrosine phosphatase.