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Biliprotein maturation: the chromophore attachment

H. Scheer, K.‐H. Zhao

Molecular Microbiology · 2008 · Review

doi:10.1111/j.1365-2958.2008.06160.x

Abstract

Summary Biliproteins are a widespread group of brilliantly coloured photoreceptors characterized by linear tetrapyrrolic chromophores, bilins, which are covalently bound to the apoproteins via relatively stable thioether bonds. Covalent binding stabilizes the chromoproteins and is mandatory for phycobilisome assembly; and, it is also important in biliprotein applications such as fluorescence labelling. Covalent binding has, on the other hand, also considerably hindered biliprotein research because autocatalytic chromophore additions are rare, and information on enzymatic addition by lyases was limited to a single example, an EF‐type lyase attaching phycocyanobilin to cysteine‐α84 of C‐phycocyanin. The discovery of new activities for the latter lyases, and of new types of lyases, have reinvigorated research activities in the subject. So far, work has mainly concentrated on cyanobacterial phycobiliproteins. Methodological advances in the process, however, as well as the finding of often large numbers of homologues, opens new possibilities for research on the subsequent assembly/disassembly of the phycobilisome in cyanobacteria and red algae, on the assembly and organization of the cryptophyte light‐harvesting system, on applications in basic research such as protein folding, and on the use of phycobiliproteins for labelling.

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    Wagner JR, Brunzelle JS, Forest KT, Vierstra RD. A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome. Nature. 2005;438:325-331.

    Not in our library10.1038/nature04118

  94. 94.

    Wang XQ, Li LN, Chang WR, Zhang JP, Gui LL, Guo BJ, Liang DC. Structure of C-phycocyanin from Spirulina platensis at 2.2 Angstrom resolution: a novel monoclinic crystal form for phycobiliproteins in phycobilisomes. Acta Cryst D Biol Cryst. 2001;57:784-792.

    Not in our library10.1107/s0907444901004528

  95. 95.

    Wemmer DE, Wedemayer GJ, Glazer AN. Phycobilins of Cryptophycean Algae – Novel Linkage of Dihydrobiliverdin in a Phycoerythrin-555 and a Phycocyanin-645. J Biol Chem. 1993;268:1658-1669.

    Not in our library

  96. 96.

    Wilbanks SM, Glazer AN. Rod structure of a phycoerythrin II-containing phycobilisome. I. Organization and sequence of the gene cluster encoding the major phycbiliprotein rod components in the genome of marine. Synechococcus SP Wh8020. J Biol Chem. 1993;268:1226-1235.

    Not in our library

  97. 97.

    Wilson KM, Morrison IE, Smith PR, Fernandez N, Cherry RJ. Single particle tracking of cell-surface HLA-DR molecules using R-phycoerythrin labeled monoclonal antibodies and fluorescence digital imaging. J Cell Sci. 1996;109:2101-2109.

    Not in our library10.1242/jcs.109.8.2101

  98. 98.

    Wu S-H, Lagarias JC. Defining the bilin lyase domain: lessons from the extended phytochrome superfamily. Biochemistry. 2000;39:13487-13495.

    Not in our library10.1021/bi001123z

  99. 99.

    Zabulon G, Richaud C, Guidi-Rontani C, Thomas J-C. NblA gene expression in synechocystis PCC 6803 strains lacking DspA (Hik33) and a NblR-like protein. Curr Microbiol. 2007;54:36-41.

    Not in our library10.1007/s00284-006-0251-y

  100. 100.

    Zhou J, Gasparich GE, Stirewalt VL, de Lorimier R, Bryant DA. The cpcE and cpcF genes of Synechococcus sp. PCC 7002. Construction and phenotypic characterization of interposon mutants. J Biol Chem. 1992;267:16138-16145.

    Not in our library

  101. 101.

    Zhao KH, Haessner R, Cmiel E, Scheer H. Type I reversible of phycoerythrocyanin involves Z/E-isomerization of α-84 phycoviolobilin chromophore. Biochim Biophys Acta. 1995;1228:235-243.

    Not in our library

  102. 102.

    Zhao KH, Wu D, Wang L, Zhou M, Storf M, Bubenzer C, et al. Characterization of phycoviolobilin phycoerythrocyanin- α84-cystein-lyase-(isomerizing) from Mastigocladus laminosus. Eur J Biochem. 2002;269:4542-4550.

    Not in our library10.1046/j.1432-1033.2002.03148.x

  103. 103.

    Zhao KH, Ran Y, Li M, Sun Y-N, Zhou M, Storf M, et al. Photochromic biliproteins from the cyanobacterium Anabaena sp. PCC 7120. lyase activities, chromophore exchange and photochromism in phytochrome and phycoerythrocyanin. Biochemistry. 2004a;43:11576-11588.

    Not in our library10.1021/bi0491548

  104. 104.

    Zhao KH, Zhu JP, Song B, Zhou M, Storf M, Böhm S, et al. Non-enzymatic chromophore attachment in biliproteins: conformational control by the detergent Triton X-100. Biochim Biophys Acta. 2004b;1657:131-145.

    Not in our library10.1016/j.bbabio.2004.04.010

  105. 105.

    Zhao KH, Su P, Böhm S, Song B, Zhou M, Bubenzer C, Scheer H. Reconstitution of phycobilisome core-membrane linker, Lcm, by autocatalytic chromophore binding to ApcE. Biochim Biophys Acta. 2005a;1706:81-87.

    Not in our library10.1016/j.bbabio.2004.09.008

  106. 106.

    Zhao KH, Wu D, Zhou M, Zhang L, Böhm S, Bubenzer C, Scheer H. Amino acid residues associated with enzymatic activity of the isomerizing phycoviolobilin-lyase PecE/F. Biochemistry. 2005b;44:8126-8137.

    Not in our library10.1021/bi0500168

  107. 107.

    Zhao K-H, Wu D, Zhang L, Zhou M, Böhm S, Bubenzer C, Scheer H. Chromophore attachment in phycocyanin: functional amino acids of phycocyanobilin: α-phycocyanin lyase and evidence for chromophore binding. FEBS J. 2006a;273:1262-1274.

    Not in our library10.1111/j.1742-4658.2006.05149.x

  108. 108.

    Zhao KH, Su P, Li JA, Tu JM, Zhou M, Bubenzer C, Scheer H. Chromophore attachment to phycobiliprotein β-subunits: phycocyanobilin: cysteine-β84 phycobiliprotein lyase activity of CpeS-like protein from Anabaena sp. PCC7120. J Biol Chem. 2006b;281:8573-8581.

    Not in our library10.1074/jbc.m513796200

  109. 109.

    Zhao KH, Su P, Tu JM, Wang X, Liu H, Plöscher M, et al. Phycobilin: cystein-84 biliprotein lyase, a near-universal lyase for cysteine-84-binding sites in cyanobacterial phycobiliproteins. Proc Natl Acad Sci USA. 2007a;104:14300-14305.

    Not in our library10.1073/pnas.0706209104

  110. 110.

    Zhao KH, Zhang J, Tu JM, Böhm S, Plöscher M, Eichacker L, et al. Lyase activities of CpcS and CpcT-like proteins from Nostoc sp. PCC7120, and sequential reconstitution of binding sites of phycoerythrocyanin and phycocyanin β-subunits. J Biol Chem. 2007b;282:34093-34103.

    Not in our library10.1074/jbc.m703038200

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