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Molecular Cloning of cpcU and Heterodimeric Bilin Lyase Activity Analysis of CpcU and CpcS for Attachment of Phycocyanobilin to Cys-82 on the β-Subunit of Phycocyanin in Arthrospira platensis FACHB314

Key Laboratory of Marine Genetics and Breeding, Ministry of Education, Ocean University of China, Qingdao 266003, China
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Academic Editor: Derek J. McPhee
Molecules 2016, 21(3), 357; https://doi.org/10.3390/molecules21030357
Received: 23 January 2016 / Revised: 8 March 2016 / Accepted: 10 March 2016 / Published: 16 March 2016
(This article belongs to the Section Molecular Diversity)
A new bilin lyase gene cpcU was cloned from Arthrospira platensis FACHB314 to study the assembly of the phycocyanin β-Subunit. Two recombinant plasmids, one contained the phycocyanobilin (PCB) producing genes (hoxI and pcyA), while the other contained the gene of the β-Subunit of phycobiliprotein (cpcB) and the lyase gene (cpcU, cpcS, or cpcU/S) were constructed and separately transferred into Escherichia coli in order to test the activities of relevant lyases for catalyzing PCB addition to CpcB during synthesizing fluorescent β-PC of A. platensis FACHB314. The fluorescence intensity examination showed that Cys-82 maybe the active site for the β-Subunit binding to PCBs and the attachment could be carried out by CpcU, CpcS, or co-expressed cpcU/S in A. platensis FACHB314. View Full-Text
Keywords: Arthrospira platensis FACHB314; CpcU; CpcS; site-directed mutation; fluorescence intensity Arthrospira platensis FACHB314; CpcU; CpcS; site-directed mutation; fluorescence intensity
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Wu, F.; Zang, X.; Zhang, X.; Zhang, R.; Huang, X.; Hou, L.; Jiang, M.; Liu, C.; Pang, C. Molecular Cloning of cpcU and Heterodimeric Bilin Lyase Activity Analysis of CpcU and CpcS for Attachment of Phycocyanobilin to Cys-82 on the β-Subunit of Phycocyanin in Arthrospira platensis FACHB314. Molecules 2016, 21, 357.

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