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Biosynthesis of fluorescent allophycocyanin alpha-subunits by autocatalytic bilin attachment

机译：通过自催化胆红素附着生物合成荧光的藻蓝蛋白α-亚基

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摘要

Allophycocyanin ( APC) is one of the phycobiliproteins expressed in cyanobacteria. Phycobiliproteins contain a covalently bound chromophore, and thus, they are valuable as fluorescent probes. Biosynthesis of a functional phycobiliprotein is achieved by a bilin attachment process between the chromophore and apoprotein. Chromophore lyases are necessary to catalyze the chromophorylation of cyanobacterial phycobiliproteins, such as C-phycocyanin, and phycoerythrocyanin. To identify the lyase that catalyzes the chromophorylation of the APC alpha-subunit ( ApcA), we searched the entire genomes of two cyanobacteria, Synechocystis sp. PCC6803 and Anabaena sp. PCC 7120; however, these genomes do not appear to encode an APC-specific chromophore lyase. In this study, chromophorylated ApcA ( chromo-ApcA) was obtained via a spontaneous bilin attachment reaction. The absorption and fluorescence characteristics of chromo-ApcA were similar to those of the native APC alpha-subunit. The extent of chromophore attachment to apo-ApcA was comparable to that of the lyase-catalyzed reactions for other phycobiliproteins. These results indicate that ApcA has autocatalytic bilin: biliprotein lyase activity.
机译：藻蓝蛋白（APC）是在蓝细菌中表达的藻胆蛋白之一。藻胆蛋白含有共价结合的生色团，因此，它们作为荧光探针是有价值的。功能性藻胆蛋白的生物合成是通过生色团和载脂蛋白之间的胆红素附着过程实现的。发色团裂解酶对于催化诸如C-藻蓝蛋白和藻红蛋白的蓝藻藻胆蛋白的发色作用是必需的。为了确定能催化APCα亚基（ApcA）的磷酸化的裂解酶，我们搜索了两个蓝细菌Synechocystis sp。的整个基因组。 PCC6803和Anabaena sp。 PCC 7120;但是，这些基因组似乎没有编码APC特异性发色团裂解酶。在这项研究中，通过自发的胆红素附着反应获得了发色的ApcA（chromo-ApcA）。 chromo-ApcA的吸收和荧光特性与天然APCα-亚基相似。发色团与apo-ApcA的附着程度与其他藻胆蛋白的裂解酶催化反应相当。这些结果表明，ApcA具有自动催化的胆红素：胆蛋白裂解酶活性。

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