The phycobilisome core-membrane linkers from Synechocystis sp. PCC 6803 and red-algae assemble in the same topology.
The phycobilisome core-membrane linkers from Synechocystis sp. PCC 6803 and red-algae assemble in the same topology.
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来自集胞藻属的藻胆体核心膜连接体。
DOI：
10.1111/tpj.15389
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发表时间：
2021-06
期刊：
影响因子：
7.2
通讯作者：
Zhao Kai-Hong
中科院分区：
文献类型：
--
作者：
Niu Nan-Nan;Lu Lu;Peng Pan-Pan;Fu Zhi-Juan;Miao Dan;Zhou Ming;Noy Dror;Zhao Kai-Hong
蓝藻和红藻的藻胆体是一种独特的百万吨级捕光蛋白质-色素复合体，它利用比林衍生物进行光吸收和能量转移。最近，红藻藻胆体的高分辨分子结构揭示了多结构域核心-膜连接子(LCM)是如何特异性地组织藻胆体核心中的别藻蓝蛋白亚基的。但是，LCM在这些结构中的拓扑结构与蓝藻藻胆体在低分辨率结构上的拓扑结构不同。特别是，蓝藻的模型假设LCM的Arm2结构域连接两个基础别藻蓝蛋白圆柱体，而红藻藻胆体结构表明Arm2部分埋在一个基础圆柱体的核心，并将其连接到顶部圆柱体。在这里，我们通过对编码LCM的APCE基因突变的生化分析表明，蓝藻和红藻的LCM拓扑结构实际上是相同的。我们发现，在LCM中移除顶端柱体连接子结构域会将PBS核心纵向分裂为两个独立的基柱体。删除ARM2 N末端的全部或部分螺旋-环-螺旋结构域，解体基柱体，并导致含有末端发射器的部分APCD的降解。删除下面的30个氨基酸环严重影响了基柱的组装，但进一步缺失Arm2的C-末端一半氨基酸对这种组装只有很小的影响。总之，生化数据与红藻LCM拓扑结构一致，表明蓝藻和红藻中的PBS核心以相同的方式组装。
The phycobilisomes of cyanobacteria and red-algae are unique megadaltons light-harvesting protein-pigment complexes that utilize bilin derivatives for light absorption and energy transfer. Recently, the high-resolution molecular structures of red-algal phycobilisomes revealed how the multi-domain core-membrane linker (LCM ) specifically organizes the allophycocyanin subunits in the phycobilisome's core. But, the topology of LCM in these structures was different than the one suggested for cyanobacterial phycobilisomes based on lower resolution structures. Particularly, the model for cyanobacteria assumed that the Arm2 domain of LCM connects the two basal allophycocyanin cylinders whereas the red-algal phycobilisome structures revealed that Arm2 is partly buried in the core of one basal cylinder and connects it to the top cylinder. Here, we show by biochemical analysis of mutations in the apcE gene that encodes LCM , that the cyanobacterial and red-algal LCM topologies are actually the same. We found that removing the top cylinder linker domain in LCM splits the PBS core longitudinally into two separate basal cylinders. Deleting either all or part of the helix-loop-helix domain at the N-terminal end of Arm2, disassembled the basal cylinders and resulted in degradation of the part containing the terminal emitter, ApcD. Deleting the following 30 amino-acids loop severely affected the assembly of the basal cylinders, but further deletion of the amino-acids at the C-terminal half of Arm2 had only minor effects on this assembly. Altogether, the biochemical data is consistent with the red-algal LCM topology suggesting that the PBS cores in cyanobacteria and red-algae assemble in the same way.
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影响因子：
64.8
作者：
Ma, Jianfei;You, Xin;Sui, Sen-Fang
通讯作者：
Sui, Sen-Fang
影响因子：
4.3
作者：
Arteni, Ana A.;Ajlani, Ghada;Boekema, Egbert J.
通讯作者：
Boekema, Egbert J.
DOI：
10.1007/978-981-10-7757-9_3
发表时间：
2018-01-01
期刊：
MEMBRANE PROTEIN COMPLEXES: STRUCTURE AND FUNCTION
影响因子：
--
作者：
Harris, Dvir;Bar-Zvi, Shira;Adir, Noam
通讯作者：
Adir, Noam
影响因子：
13.6
作者：
Liu H;Zhang MM;Weisz DA;Cheng M;Pakrasi HB;Blankenship RE
通讯作者：
Blankenship RE
影响因子：
5.6
作者：
Ducret, A;M端ller, SA;Engel, A
通讯作者：
Engel, A