tailieunhanh - Báo cáo Y học: Two independent, light-sensing two-component systems in a filamentous cyanobacterium

Two ORFs, cphA and cphB, encoding proteins CphA and CphB with strong similarities to plant phytochromes and to the cyanobacterial phytochrome Cph1 of Synechocystis sp. PCC 6803 have been identified in the filamentous cyanobacterium Calothrix sp. PCC7601. While CphA carries a cysteine within a highly conserved amino-acid sequence motif, to which the chromophore phytochromobilin is covalently bound in plant phytochromes, in CphB this position is changed into a leucine. Both ORFs are followed by rcpA and rcpB genes encoding response regulator proteins similar to those known from the bacterial two-component signal transduction. In Calothrix, all four genes are expressed under. | Eur. J. Biochem. 269 2662-2671 2002 FEBS 2002 doi Two independent light-sensing two-component systems in a filamentous cyanobacterium Helena J. M. M. Jorissen1. Beniamin Quest2 Ania Remberg1. Therese Coursin3. Silvia E Braslavsky1. Kurt Schaffner1 Nicole Tandeau de Marsac3 and Wolfgang Gartner1 2 1 Max-Planck-Institut fur Strahlenchemie Millheim an der Ruhr Germany 2Max-Planck-Institut fur Biochemie Martinsried Germany 3 Unite des Cyanobacteries Departement de Microbiologie Fondamentale et Medicale Institut Pasteur URA-CNRS 2172 Paris France Two ORFs cphA and cphB encoding proteins CphA and CphB with strong similarities to plant phytochromes and to the cyanobacterial phytochrome Cph1 of Synechocystis sp. PCC 6803 have been identified in the filamentous cyanobacterium Calothrix sp. PCC7601. While CphA carries a cysteine within a highly conserved amino-acid sequence motif to which the chromophore phytochromobilin is covalently bound in plant phytochromes in CphB this position is changed into a leucine. Both ORFs are followed by rcpA and rcpB genes encoding response regulator proteins similar to those known from the bacterial two-component signal transduction. In Calothrix all four genes are expressed under white light irradiation conditions albeit in low amounts. For heterologous expression and convenient purification the cloned genes were furnished with His-tag encoding sequences at their 3 end and expressed in Escherichia coli. The two recombinant apoproteins CphA and CphB bound the chromophore phycocyanobilin PCB in a covalent and a noncovalent manner respectively and underwent photochromic absorption changes reminiscent of the Pr and Pfr forms red and far-red absorbing forms respectively of the plant phytochromes and Cph1. A red shift in the absorption maxima of the CphB PCB complex kmax 685 and 735 nm for Pr and Pfr respectively is indicative for a noncovalent incorporation of the chromophore kmax of Pr Pfr of CphA 663 700 nm . A

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