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Phycobiliprotein Biosynthesis in Cyanobacteria: Structure and Function of Enzymes Involved in Post-translational Modification

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Recent Advances in Phototrophic Prokaryotes

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 675))

Abstract

Cyanobacterial phycobiliproteins are brilliantly colored due to the presence of covalently attached chromophores called bilins, linear tetrapyrroles derived from heme. For most phycobiliproteins, these post-translational modifications are catalyzed by enzymes called bilin lyases; these enzymes ensure that the appropriate bilins are attached to the correct cysteine residues with the proper stereochemistry on each phycobiliprotein subunit. Phycobiliproteins also contain a unique, post-translational modification, the methylation of a conserved asparagine (Asn) present at β-72, which occurs on the β-subunits of all phycobiliproteins. We have identified and characterized several new families of bilin lyases, which are responsible for attaching PCB to phycobiliproteins as well as the Asn methyl transferase for β-subunits in Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803. All of the enzymes responsible for synthesis of holo-phycobiliproteins are now known for this cyanobacterium, and a brief discussion of each enzyme family and its role in the biosynthesis of phycobiliproteins is presented here. In addition, the first structure of a bilin lyase has recently been solved (PDB ID: 3BDR). This structure shows that the bilin lyases are most similar to the lipocalin protein structural family, which also includes the bilin-binding protein found in some butterflies.

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Acknowledgments

This research was supported by National Science Foundation grants to W. M. S. (MCB-0133441 and MCB-0843664) and to D. A. B. (MCB-0077586 and MCB-0519743). We would like to thank Farhad Forouhar and John Hunt from Columbia University for preparing the image shown in Fig. 12.6.

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  1. Department of Biological Sciences, University of New Orleans, New Orleans, LA, 70148, USA

    Wendy M. Schluchter, Avijit Biswas, Nicolle A. Saunée, Shervonda R. Williams & Crystal A. Mille

  2. Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA

    Gaozhong Shen, Richard M. Alvey & Donald A. Bryant

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  1. Wendy M. Schluchter
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Correspondence to Wendy M. Schluchter .

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Schluchter, W.M. et al. (2010). Phycobiliprotein Biosynthesis in Cyanobacteria: Structure and Function of Enzymes Involved in Post-translational Modification. In: Hallenbeck, P. (eds) Recent Advances in Phototrophic Prokaryotes. Advances in Experimental Medicine and Biology, vol 675. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-1528-3_12

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