华中师范大学学报（自然科学版）2012，Vol.46Issue(5)：606-610,638,6.
重组蓝细菌藻蓝蛋白RpcA共价偶联多种藻胆色素
Covalent attachment of various phycobilins to recombinant cyanobacteria phycocyanin RpcA
摘要
Abstract
Researchers have discovered the enzymes that synthesize phycobilin chromo-phores as well as many of the phycobilin lyase enzymes that attach these chromophores to their apoproteins. Here by conveniently heterologous expression in Escherichia coli, all four phycobilins in cyanobacterium were respectively covalently attached to a subunit of phycocyanin from the marine cyanobacterium Synechococcus sp. WH8102. The lyase-Isomerase RpcG used PEB or PCB as substrates and attach them, with concomitant isomerization, to RpcA, respectively producing PUB-RpcA or PVB-RpcA. But the bilin lyases CpcE/CpcF took PEB or PCB as substrates and attach them, without isomerization, to RpcA, respectively forming PEB-RpcA or PCB-RpcA. The latter exhibited a high-fluorescence quantum yield. Two lyases used two bilin substrates and produced four distinct chromoproteins, respectively bound to the same RpcA. A comparison between RpcG and CpcE/CpcF can investigate the structural basis of isomerization. At the same time, these biliproteins have potential application in fluorescent biological markers.关键词
藻胆蛋白/藻胆色素/体内重组Key words
phycobiliprotein/ phycobilin/ reconstitution in vivo分类
生物科学引用本文复制引用
伍贤军,邓明刚,赵开弘,周明..重组蓝细菌藻蓝蛋白RpcA共价偶联多种藻胆色素[J].华中师范大学学报（自然科学版）,2012,46(5):606-610,638,6.基金项目
国家自然科学基金项目(30870519 （）
21072068). （）
