دورية أكاديمية

Molecular bases of an alternative dual-enzyme system for light color acclimation of marine Synechococcus cyanobacteria.

التفاصيل البيبلوغرافية
العنوان: Molecular bases of an alternative dual-enzyme system for light color acclimation of marine Synechococcus cyanobacteria.
المؤلفون: Grébert T; Ecology of Marine Plankton Team, UMR 7144 Adaptation and Diversity in the Marine Environment, Station Biologique, Sorbonne Université, CNRS, 29680 Roscoff, France., Nguyen AA; Department of Biological Sciences, University of New Orleans, New Orleans, LA 70148.; Department of Chemistry, University of New Orleans, New Orleans, LA 70148., Pokhrel S; Department of Biological Sciences, University of New Orleans, New Orleans, LA 70148., Joseph KL; Department of Biological Sciences, University of New Orleans, New Orleans, LA 70148., Ratin M; Ecology of Marine Plankton Team, UMR 7144 Adaptation and Diversity in the Marine Environment, Station Biologique, Sorbonne Université, CNRS, 29680 Roscoff, France., Dufour L; Ecology of Marine Plankton Team, UMR 7144 Adaptation and Diversity in the Marine Environment, Station Biologique, Sorbonne Université, CNRS, 29680 Roscoff, France., Chen B; Department of Biology, Indiana University, Bloomington, IN 47405., Haney AM; Department of Biology, Indiana University, Bloomington, IN 47405., Karty JA; Department of Chemistry, Indiana University, Bloomington, IN 47405., Trinidad JC; Department of Chemistry, Indiana University, Bloomington, IN 47405., Garczarek L; Ecology of Marine Plankton Team, UMR 7144 Adaptation and Diversity in the Marine Environment, Station Biologique, Sorbonne Université, CNRS, 29680 Roscoff, France., Schluchter WM; Department of Biological Sciences, University of New Orleans, New Orleans, LA 70148., Kehoe DM; Department of Biology, Indiana University, Bloomington, IN 47405., Partensky F; Ecology of Marine Plankton Team, UMR 7144 Adaptation and Diversity in the Marine Environment, Station Biologique, Sorbonne Université, CNRS, 29680 Roscoff, France; frederic.partensky@sb-roscoff.fr.
المصدر: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2021 Mar 02; Vol. 118 (9).
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print Cited Medium: Internet ISSN: 1091-6490 (Electronic) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : National Academy of Sciences
مواضيع طبية MeSH: Bacterial Proteins/*metabolism , Light-Harvesting Protein Complexes/*metabolism , Lyases/*metabolism , Phycocyanin/*biosynthesis , Phycoerythrin/*biosynthesis , Pigments, Biological/*biosynthesis , Synechococcus/*metabolism, Acclimatization ; Aquatic Organisms ; Bacterial Proteins/genetics ; Cloning, Molecular ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression Regulation, Bacterial ; Genetic Complementation Test ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Genomic Islands ; Light ; Light-Harvesting Protein Complexes/genetics ; Lyases/genetics ; Phycobilins/biosynthesis ; Phycobilins/genetics ; Phycocyanin/genetics ; Phycoerythrin/genetics ; Phylogeny ; Pigments, Biological/genetics ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Synechococcus/classification ; Synechococcus/genetics ; Synechococcus/radiation effects ; Urobilin/analogs & derivatives ; Urobilin/biosynthesis ; Urobilin/genetics
مستخلص: Marine Synechococcus cyanobacteria owe their ubiquity in part to the wide pigment diversity of their light-harvesting complexes. In open ocean waters, cells predominantly possess sophisticated antennae with rods composed of phycocyanin and two types of phycoerythrins (PEI and PEII). Some strains are specialized for harvesting either green or blue light, while others can dynamically modify their light absorption spectrum to match the dominant ambient color. This process, called type IV chromatic acclimation (CA4), has been linked to the presence of a small genomic island occurring in two configurations (CA4-A and CA4-B). While the CA4-A process has been partially characterized, the CA4-B process has remained an enigma. Here we characterize the function of two members of the phycobilin lyase E/F clan, MpeW and MpeQ, in Synechococcus sp. strain A15-62 and demonstrate their critical role in CA4-B. While MpeW, encoded in the CA4-B island and up-regulated in green light, attaches the green light-absorbing chromophore phycoerythrobilin to cysteine-83 of the PEII α-subunit in green light, MpeQ binds phycoerythrobilin and isomerizes it into the blue light-absorbing phycourobilin at the same site in blue light, reversing the relationship of MpeZ and MpeY in the CA4-A strain RS9916. Our data thus reveal key molecular differences between the two types of chromatic acclimaters, both highly abundant but occupying distinct complementary ecological niches in the ocean. They also support an evolutionary scenario whereby CA4-B island acquisition allowed former blue light specialists to become chromatic acclimaters, while former green light specialists would have acquired this capacity by gaining a CA4-A island.
Competing Interests: The authors declare no competing interest.
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فهرسة مساهمة: Keywords: light regulation; marine cyanobacteria; photosynthesis; phycobilin lyase; phycoerythrin
المشرفين على المادة: 0 (Bacterial Proteins)
0 (Light-Harvesting Protein Complexes)
0 (Phycobilins)
0 (Pigments, Biological)
0 (Protein Subunits)
0 (Recombinant Proteins)
11016-15-2 (Phycocyanin)
11016-17-4 (Phycoerythrin)
18097-67-1 (phycoerythrobilin)
1856-98-0 (Urobilin)
61932-71-6 (phycourobilin)
EC 4.- (Lyases)
تواريخ الأحداث: Date Created: 20210225 Date Completed: 20210804 Latest Revision: 20210825
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC7936332
DOI: 10.1073/pnas.2019715118
PMID: 33627406
قاعدة البيانات: MEDLINE
الوصف
تدمد:1091-6490
DOI:10.1073/pnas.2019715118