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Full-Text Articles in Life Sciences
Cpet Is The Phycoerythrobilin Lyase For Cys-165 On Beta-Phycoerythrin From Fremyella Diplosiphon And The Chaperone-Like Protein Cpez Greatly Improves Its Activity., Wendy M. Schluchter, A. A. Nguyen, K. L. Joseph, A. N. Bussell, S. Pokhrel, A. J. Karty, M. C. Kronfel, D. M. Kehoe
Cpet Is The Phycoerythrobilin Lyase For Cys-165 On Beta-Phycoerythrin From Fremyella Diplosiphon And The Chaperone-Like Protein Cpez Greatly Improves Its Activity., Wendy M. Schluchter, A. A. Nguyen, K. L. Joseph, A. N. Bussell, S. Pokhrel, A. J. Karty, M. C. Kronfel, D. M. Kehoe
Biological Sciences Faculty Publications
Bilin lyases are enzymes which ligate linear tetrapyrrole chromophores to specific cysteine residues on light harvesting proteins present in cyanobacteria and red algae. The lyases responsible for chromophorylating the light harvesting protein phycoerythrin (PE) have not been fully characterized. In this study, we explore the role of CpeT, a putative bilin lyase, in the biosynthesis of PE in the cyanobacterium Fremyella diplosiphon. Recombinant protein studies show that CpeT alone can bind phycoerythrobilin (PEB), but CpeZ, a chaperone-like protein, is needed in order to correctly and efficiently attach PEB to the beta-subunit of PE. MS analyses of the recombinant beta-subunit of …
Cpef Is The Bilin Lyase That Ligates The Doubly Linked Phycoerythrobilin On Phycoerythrin In The Cyanobacterium Fremyella Diplosiphon, Wendy M. Schluchter, R. B. Cole, D. M. Kehoe, M. N. Boutaghou, J. A. Karty, A. Gutu, L. S. Hernandez, J. P. Frick, C. V. Hernandez, C. M. Kronfel
Cpef Is The Bilin Lyase That Ligates The Doubly Linked Phycoerythrobilin On Phycoerythrin In The Cyanobacterium Fremyella Diplosiphon, Wendy M. Schluchter, R. B. Cole, D. M. Kehoe, M. N. Boutaghou, J. A. Karty, A. Gutu, L. S. Hernandez, J. P. Frick, C. V. Hernandez, C. M. Kronfel
Biological Sciences Faculty Publications
Phycoerythrin (PE) is a green light-absorbing protein present in the light-harvesting complex of cyanobacteria and red algae. The spectral characteristics of PE are due to its prosthetic groups, or phycoerythrobilins (PEBs), that are covalently attached to the protein chain by specific bilin lyases. Only two PE lyases have been identified and characterized so far, and the other bilin lyases are unknown. Here, using in silico analyses, markerless deletion, biochemical assays with purified and recombinant proteins, and site-directed mutagenesis, we examined the role of a putative lyase-encoding gene, cpeF, in the cyanobacterium Fremyella diplosiphon. Analyzing the phenotype of the cpeF deletion, …
The Roles Of The Chaperone-Like Protein Cpez And The Phycoerythrobilin Lyase Cpey In Phycoerythrin Biogenesis, Wendy M. Schluchter, D. M. Kehoe, J. A. Karty, T. Blensdorf, A. Gutu, J. P. Frick, A. Biswas, C. M. Kronfel
The Roles Of The Chaperone-Like Protein Cpez And The Phycoerythrobilin Lyase Cpey In Phycoerythrin Biogenesis, Wendy M. Schluchter, D. M. Kehoe, J. A. Karty, T. Blensdorf, A. Gutu, J. P. Frick, A. Biswas, C. M. Kronfel
Biological Sciences Faculty Publications
Phycoerythrin (PE) present in the distal ends of light-harvesting phycobilisome rods in Fremyella diplosiphon (Tolypothrix sp. PCC 7601) contains five phycoerythrobilin (PEB) chromophores attached to six cysteine residues for efficient green light capture for photosynthesis. Chromophore ligation on PE subunits occurs through bilin lyase catalyzed reactions, but the characterization of the roles of all bilin lyases for phycoerythrin is not yet complete. To gain a more complete understanding about the individual functions of CpeZ and CpeY in PE biogenesis in cyanobacteria, we examined PE and phycobilisomes purified from wild type F. diplosiphon, cpeZ and cpeY knockout mutants. We find that …
Adaptation To Blue Light In Marine Synechococcus Requires Mpeu, An Enzyme With Similarity To Phycoerythrobilin Lyase Isomerases, Wendy M. Schluchter, Rania Mohamed Mahmoud, Joseph Sanfilippo, Adam A. Nguyen, Johann A. Strnat, Frédéric Partensky, Laurence Garczarek, Nabil Kassem, David M. Kehoe
Adaptation To Blue Light In Marine Synechococcus Requires Mpeu, An Enzyme With Similarity To Phycoerythrobilin Lyase Isomerases, Wendy M. Schluchter, Rania Mohamed Mahmoud, Joseph Sanfilippo, Adam A. Nguyen, Johann A. Strnat, Frédéric Partensky, Laurence Garczarek, Nabil Kassem, David M. Kehoe
Biological Sciences Faculty Publications
Marine Synechococcus has successfully adapted to environments with different light colors, which likely contributes to this genus being the second most abundant group of microorganisms worldwide. Populations of Synechococcus that grow in deep, blue ocean waters contain large amounts of the blue-light absorbing chromophore phycourobilin (PUB) in their light harvesting complexes (phycobilisomes). Here, we show that all Synechococcus strains adapted to blue light possess a gene called mpeU. MpeU is structurally similar to phycobilin lyases, enzymes that ligate chromophores to phycobiliproteins. Interruption of mpeU caused a reduction in PUB content, impaired phycobilisome assembly and reduced growth rate more strongly in …