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首页> 外文期刊>Journal of bacteriology >Structural and Mutational Analysis of Band 7 Proteins in the Cyanobacterium Synechocystis sp. Strain PCC 6803
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Structural and Mutational Analysis of Band 7 Proteins in the Cyanobacterium Synechocystis sp. Strain PCC 6803

机译：蓝藻蓝藻中带7蛋白的结构和突变分析。应变PCC 6803

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Band 7 proteins, which encompass members of the stomatin, prohibitin, flotillin, and HflK/C protein families, are integral membrane proteins that play important physiological roles in eukaryotes but are poorly characterized in bacteria. We have studied the band 7 proteins encoded by the cyanobacterium Synechocystis sp. strain PCC 6803, with emphasis on their structure and proposed role in the assembly and maintenance of the photosynthetic apparatus. Mutagenesis revealed that none of the five band 7 proteins (Slr1106, Slr1128, Slr1768, Sll0815, and Sll1021) was essential for growth under a range of conditions (including high light, salt, oxidative, and temperature stresses), although motility was compromised in an Slr1768 inactivation mutant. Accumulation of the major photosynthetic complexes in the thylakoid membrane and repair of the photosystem II complex following light damage were similar in the wild type and a quadruple mutant. Cellular fractionation experiments indicated that three of the band 7 proteins (Slr1106, Slr1768, and Slr1128) were associated with the cytoplasmic membrane, whereas Slr1106, a prohibitin homologue, was also found in the thylakoid membrane fraction. Blue native gel electrophoresis indicated that these three proteins, plus Sll0815, formed large (>669-kDa) independent complexes. Slr1128, a stomatin homologue, has a ring-like structure with an approximate diameter of 16 nm when visualized by negative stain electron microscopy. No evidence for band 7/FtsH supercomplexes was found. Overall, our results indicate that the band 7 proteins form large homo-oligomeric complexes but do not play a crucial role in the biogenesis of the photosynthetic apparatus in Synechocystis sp. strain PCC 6803.
机译：Band 7蛋白，包括Stomatin，Probidin，Flotilin和HflK / C蛋白家族的成员，是必不可少的膜蛋白，在真核生物中起着重要的生理作用，但在细菌中的表征却很差。我们研究了由蓝细菌 Synechocystis sp编码的7带蛋白。菌株PCC 6803，重点在于其结构以及在光合作用设备的组装和维护中的拟议作用。诱变显示，虽然在以下条件下（包括强光，盐，氧化和温度胁迫）条件下的生长，五个带7蛋白（Slr1106，Slr1128，Slr1768，Sll0815和Sll1021）都不对生长至关重要。 Slr1768失活突变体。在野生型和四倍体突变体中，类囊体膜中主要光合复合物的积累和光损伤后光系统II复合物的修复相似。细胞分级分离实验表明，带7蛋白中的三个（Slr1106，Srr1768和Slr1128）与细胞质膜相关，而在类囊体膜级分中也发现了禁止蛋白的同源物Slr1106。蓝色天然凝胶电泳表明，这三种蛋白质以及Sll0815形成了大的（> 669-kDa）独立复合物。 Slr1128是一种抑菌素的同源物，当通过负染色电子显微镜观察时，具有约16 nm直径的环状结构。没有发现带7 / FtsH超复合物的证据。总体而言，我们的结果表明，带7蛋白形成大的同型寡聚复合物，但在 sp。的光合作用的生物合成中不发挥关键作用。株PCC 6803。

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