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• W1580451511 abstract "Bacteriophytochromes constitute a light‐sensing subgroup of sensory kinases with a chromophore‐binding motif in the N‐terminal half and a C‐terminally located histidine kinase activity. The cyanobacterium Fremyella diplosiphon (also designated Calothrix sp.) expresses two sequentially very similar bacteriophytochromes, cyanobacterial phytochrome A (CphA) and cyanobacterial phytochrome B (CphB). Cyanobacterial phytochrome A has the canonical cysteine residue, by which covalent chromophore attachment is accomplished in the same manner as in plant phytochromes; however, its paralog cyanobacterial phytochrome B carries a leucine residue at that position. On the basis of in vitro experiments that showed, for both cyanobacterial phytochrome A and cyanobacterial phytochrome B, light‐induced autophosphorylation and phosphate transfer to their cognate response regulator proteins RcpA and RcpB [Hübschmann T, Jorissen HJMM, Börner T, Gärtner W & deMarsac NT (2001) Eur J Biochem 268 , 3383–3389], we aimed at the identification of a chromophore that is incorporated in vivo into cyanobacterial phytochrome B within the cyanobacterial cell. The approach was based on the introduction of a copy of cphB into the cyanobacterium via triparental conjugation. The His‐tagged purified, recombinant protein (CphB cy ) showed photoreversible absorption bands similar to those of plant and bacterial phytochromes, but with remarkably red‐shifted maxima [ λ max 700 and 748 nm, red‐absorbing (P r ) and far red‐absorbing (P fr ) forms of phytochrome, respectively]. A comparison of the absorption maxima with those of the heterologously generated apoprotein, assembled with phycocyanobilin ( λ max 686 and 734 nm) or with biliverdin IXα (λ max 700 and 750 ± 2 nm), shows biliverdin IXα to be a genuine chromophore. The kinase activity of CphB cy and phosphotransfer to its cognate response regulator was found to be strictly P r ‐dependent. As an N‐terminally located cysteine was found as an alternative covalent binding site for several bacteriophytochrome photoreceptors that bind biliverdin and lack the canonical cysteine residue (e.g. Agrobacterium tumefaciens and Deinococcus radiodurans ), this corresponding residue in heterologously expressed cyanobacterial phytochrome B was mutated into a serine (C24S); however, there was no change in its spectral properties. On the other hand, the mutation of His267, which is located directly after the canonical cysteine, into alanine (H267A), caused complete loss of the capability of cyanobacterial phytochrome B to form a chromoprotein." @default.
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• W1580451511 date "2007-03-27" @default.
• W1580451511 modified "2023-10-18" @default.
• W1580451511 title "Homologous expression of a bacterial phytochrome" @default.
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• W1580451511 doi "https://doi.org/10.1111/j.1742-4658.2007.05751.x" @default.
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