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The phycoerythrobilin isomerization activity of MpeV in Synechococcus sp. WH8020 is prevented by the presence of a histidine at position 141 within its phycoerythrin-I β-subunit substrate

Marine Synechococcus efficiently harvest available light for photosynthesis using complex antenna systems, called phycobilisomes, composed of an allophycocyanin core surrounded by rods, which in the open ocean are always constituted of phycocyanin and two phycoerythrin (PE) types: PEI and PEII. Thes...

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Autores principales: Carrigee, Lyndsay A., Frick, Jacob P., Liu, Xindi, Karty, Jonathan A., Trinidad, Jonathan C., Tom, Irin P., Yang, Xiaojing, Dufour, Louison, Partensky, Frédéric, Schluchter, Wendy M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9705338/
https://www.ncbi.nlm.nih.gov/pubmed/36458192
http://dx.doi.org/10.3389/fmicb.2022.1011189
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author Carrigee, Lyndsay A.
Frick, Jacob P.
Liu, Xindi
Karty, Jonathan A.
Trinidad, Jonathan C.
Tom, Irin P.
Yang, Xiaojing
Dufour, Louison
Partensky, Frédéric
Schluchter, Wendy M.
author_facet Carrigee, Lyndsay A.
Frick, Jacob P.
Liu, Xindi
Karty, Jonathan A.
Trinidad, Jonathan C.
Tom, Irin P.
Yang, Xiaojing
Dufour, Louison
Partensky, Frédéric
Schluchter, Wendy M.
author_sort Carrigee, Lyndsay A.
collection PubMed
description Marine Synechococcus efficiently harvest available light for photosynthesis using complex antenna systems, called phycobilisomes, composed of an allophycocyanin core surrounded by rods, which in the open ocean are always constituted of phycocyanin and two phycoerythrin (PE) types: PEI and PEII. These cyanobacteria display a wide pigment diversity primarily resulting from differences in the ratio of the two chromophores bound to PEs, the green-light absorbing phycoerythrobilin and the blue-light absorbing phycourobilin. Prior to phycobiliprotein assembly, bilin lyases post-translationally catalyze the ligation of phycoerythrobilin to conserved cysteine residues on α- or β-subunits, whereas the closely related lyase-isomerases isomerize phycoerythrobilin to phycourobilin during the attachment reaction. MpeV was recently shown in Synechococcus sp. RS9916 to be a lyase-isomerase which doubly links phycourobilin to two cysteine residues (C50 and C61; hereafter C50, 61) on the β-subunit of both PEI and PEII. Here we show that Synechococcus sp. WH8020, which belongs to the same pigment type as RS9916, contains MpeV that demonstrates lyase-isomerase activity on the PEII β-subunit but only lyase activity on the PEI β-subunit. We also demonstrate that occurrence of a histidine at position 141 of the PEI β-subunit from WH8020, instead of a leucine in its counterpart from RS9916, prevents the isomerization activity by WH8020 MpeV, showing for the first time that both the substrate and the enzyme play a role in the isomerization reaction. We propose a structural-based mechanism for the role of H141 in blocking isomerization. More generally, the knowledge of the amino acid present at position 141 of the β-subunits may be used to predict which phycobilin is bound at C50, 61 of both PEI and PEII from marine Synechococcus strains.
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spelling pubmed-97053382022-11-30 The phycoerythrobilin isomerization activity of MpeV in Synechococcus sp. WH8020 is prevented by the presence of a histidine at position 141 within its phycoerythrin-I β-subunit substrate Carrigee, Lyndsay A. Frick, Jacob P. Liu, Xindi Karty, Jonathan A. Trinidad, Jonathan C. Tom, Irin P. Yang, Xiaojing Dufour, Louison Partensky, Frédéric Schluchter, Wendy M. Front Microbiol Microbiology Marine Synechococcus efficiently harvest available light for photosynthesis using complex antenna systems, called phycobilisomes, composed of an allophycocyanin core surrounded by rods, which in the open ocean are always constituted of phycocyanin and two phycoerythrin (PE) types: PEI and PEII. These cyanobacteria display a wide pigment diversity primarily resulting from differences in the ratio of the two chromophores bound to PEs, the green-light absorbing phycoerythrobilin and the blue-light absorbing phycourobilin. Prior to phycobiliprotein assembly, bilin lyases post-translationally catalyze the ligation of phycoerythrobilin to conserved cysteine residues on α- or β-subunits, whereas the closely related lyase-isomerases isomerize phycoerythrobilin to phycourobilin during the attachment reaction. MpeV was recently shown in Synechococcus sp. RS9916 to be a lyase-isomerase which doubly links phycourobilin to two cysteine residues (C50 and C61; hereafter C50, 61) on the β-subunit of both PEI and PEII. Here we show that Synechococcus sp. WH8020, which belongs to the same pigment type as RS9916, contains MpeV that demonstrates lyase-isomerase activity on the PEII β-subunit but only lyase activity on the PEI β-subunit. We also demonstrate that occurrence of a histidine at position 141 of the PEI β-subunit from WH8020, instead of a leucine in its counterpart from RS9916, prevents the isomerization activity by WH8020 MpeV, showing for the first time that both the substrate and the enzyme play a role in the isomerization reaction. We propose a structural-based mechanism for the role of H141 in blocking isomerization. More generally, the knowledge of the amino acid present at position 141 of the β-subunits may be used to predict which phycobilin is bound at C50, 61 of both PEI and PEII from marine Synechococcus strains. Frontiers Media S.A. 2022-11-15 /pmc/articles/PMC9705338/ /pubmed/36458192 http://dx.doi.org/10.3389/fmicb.2022.1011189 Text en Copyright © 2022 Carrigee, Frick, Liu, Karty, Trinidad, Tom, Yang, Dufour, Partensky and Schluchter. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Carrigee, Lyndsay A.
Frick, Jacob P.
Liu, Xindi
Karty, Jonathan A.
Trinidad, Jonathan C.
Tom, Irin P.
Yang, Xiaojing
Dufour, Louison
Partensky, Frédéric
Schluchter, Wendy M.
The phycoerythrobilin isomerization activity of MpeV in Synechococcus sp. WH8020 is prevented by the presence of a histidine at position 141 within its phycoerythrin-I β-subunit substrate
title The phycoerythrobilin isomerization activity of MpeV in Synechococcus sp. WH8020 is prevented by the presence of a histidine at position 141 within its phycoerythrin-I β-subunit substrate
title_full The phycoerythrobilin isomerization activity of MpeV in Synechococcus sp. WH8020 is prevented by the presence of a histidine at position 141 within its phycoerythrin-I β-subunit substrate
title_fullStr The phycoerythrobilin isomerization activity of MpeV in Synechococcus sp. WH8020 is prevented by the presence of a histidine at position 141 within its phycoerythrin-I β-subunit substrate
title_full_unstemmed The phycoerythrobilin isomerization activity of MpeV in Synechococcus sp. WH8020 is prevented by the presence of a histidine at position 141 within its phycoerythrin-I β-subunit substrate
title_short The phycoerythrobilin isomerization activity of MpeV in Synechococcus sp. WH8020 is prevented by the presence of a histidine at position 141 within its phycoerythrin-I β-subunit substrate
title_sort phycoerythrobilin isomerization activity of mpev in synechococcus sp. wh8020 is prevented by the presence of a histidine at position 141 within its phycoerythrin-i β-subunit substrate
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9705338/
https://www.ncbi.nlm.nih.gov/pubmed/36458192
http://dx.doi.org/10.3389/fmicb.2022.1011189
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