Amino acid sequence of the 8-kDa protein in photosystem I reaction center complex from a thermophilic cyanobacterium, Synechococcus elongatus.

Protein sequences & data analysis Pub Date : 1991-12-01
C S Jone, N Kotani, K Aso, L Yang, I Enami, K Kondo, A Tsugita
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Abstract

The 8-kDa protein in Photosystem I (PS I) reaction center complex was isolated from a thermophilic cyanobacterium, Synechococcus elongatus, by SDS-polyacrylamide gel electrophoresis using TRIS-Tricine buffer system. The complete amino acid sequence of the protein was determined. The 8-kDa protein consisted of 73 amino acid residues giving a calculated molecular weight of 7,472. No significant sequence homology were observed with the known other small subunits in PS I reaction center complex, except for the 6.5-kDa protein in PS I from another thermophilic cyanobacterium, S. vulcanus. The 8-kDa protein was characteristically rich in hydrophobic amino acid residues, especially the content of leucine. These suggest that the 8-kDa subunit is an intrinsic structure component in PS I core complex for stabilization of the reaction center.

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嗜热蓝藻长聚球菌光系统I反应中心复合体中8kda蛋白的氨基酸序列。
采用sds -聚丙烯酰胺凝胶电泳技术,利用TRIS-Tricine缓冲体系,从嗜热蓝藻长聚球菌(Synechococcus elongatus)中分离出光系统I (PS I)反应中心络合物中的8kda蛋白。测定了该蛋白的完整氨基酸序列。该8 kda蛋白由73个氨基酸残基组成,计算分子量为7,472。除了来自另一种嗜热蓝藻S. vulcanus的PS I中的6.5 kda蛋白外,与已知的PS I反应中心复合物的其他小亚基没有明显的序列同源性。8-kDa蛋白具有丰富的疏水氨基酸残基,特别是亮氨酸的含量。这表明8kda亚基是PS I核心配合物中稳定反应中心的固有结构成分。
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