ArticleThe Journal of biological chemistry2014
Insights into the biosynthesis and assembly of cryptophycean phycobiliproteins.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 52 citations in OpenAlex.
- Phycocyanobilin biosynthesis in Galdieria sulphuraria requires isomerization of phycoerythrobilin synthesized by bilin reductases.The FEBS journal · 2026Article
- Convenient Preparation and Energy Transfer Kinetic Process Verification by Ultrafast Time-resolved Fluorescence Spectra for Natural Cryptophyte Phycocyanin 645.Journal of fluorescence · 2026Article
- Structural insights into a PSI-ACPI supercomplex from a cryptophyte alga Chroomonas placoidea.Photosynthesis research · 2025Article
- Structure and distinct supramolecular organization of a PSII-ACPII dimer from a cryptophyte alga Chroomonas placoidea.Nature communications · 2024Article
- Molecular dissection of the soluble photosynthetic antenna from the cryptophyte alga Hemiselmis andersenii.Communications biology · 2023Article
- The Unique Light-Harvesting System of the Algal Phycobilisome: Structure, Assembly Components, and Functions.International journal of molecular sciences · 2023Review
- Crystal structure and molecular mechanism of an E/F type bilin lyase-isomerase.Structure (London, England : 1993) · 2022Article
- Controllable Phycobilin Modification: An Alternative Photoacclimation Response in Cryptophyte Algae.ACS central science · 2022Article
- The phycoerythrobilin isomerization activity of MpeV inFrontiers in microbiology · 2022Article
- Crystal structure of the first eukaryotic bilin reductaseThe Journal of biological chemistry · 2019Article
- Structures and enzymatic mechanisms of phycobiliprotein lyases CpcE/F and PecE/F.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Ferredoxin-dependent bilin reductases in eukaryotic algae: Ubiquity and diversity.Journal of plant physiology · 2017Article
- Distinct Features of Cyanophage-encoded T-type Phycobiliprotein Lyase ΦCpeT: THE ROLE OF AUXILIARY METABOLIC GENES.The Journal of biological chemistry · 2017Article
- Adaptation to Blue Light in MarineFrontiers in microbiology · 2017Article
- Recent advances in production, purification and applications of phycobiliproteins.World journal of biological chemistry · 2016Review
- Structure and mechanism of the phycobiliprotein lyase CpcT.The Journal of biological chemistry · 2014Article
- MpeV is a lyase isomerase that ligates a doubly linked phycourobilin on the β-subunit of phycoerythrin I and II in marine Synechococcus.The Journal of biological chemistryArticle
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phycobiliproteins are employed by cyanobacteria, red algae, glaucophytes, and cryptophytes for light-harvesting and consist of apoproteins covalently associated with open-chain tetrapyrrole chromophores. Although the majority of organisms assemble the individual phycobiliproteins into larger aggregates called phycobilisomes, members of the cryptophytes use a single type of phycobiliprotein that is localized in the thylakoid lumen. The cryptophyte Guillardia theta (Gt) uses phycoerythrin PE545 utilizing the uncommon chromophore 15,16-dihydrobiliverdin (DHBV) in addition to phycoerythrobilin (PEB). Both the biosynthesis and the attachment of chromophores to the apophycobiliprotein have not yet been investigated for cryptophytes. In this study, we identified and characterized enzymes involved in PEB biosynthesis. In addition, we present the first in-depth biochemical characterization of a eukaryotic phycobiliprotein lyase (GtCPES). Plastid-encoded HO (GtHo) was shown to convert heme into biliverdin IXα providing the substrate with a putative nucleus-encoded DHBV:ferredoxin oxidoreductase (GtPEBA). A PEB:ferredoxin oxidoreductase (GtPEBB) was found to convert DHBV to PEB, which is the substrate for the phycobiliprotein lyase GtCPES. The x-ray structure of GtCPES was solved at 2.0 Å revealing a 10-stranded β-barrel with a modified lipocalin fold. GtCPES is an S-type lyase specific for binding of phycobilins with reduced C15=C16 double bonds (DHBV and PEB). Site-directed mutagenesis identified residues Glu-136 and Arg-146 involved in phycobilin binding. Based on the crystal structure, a model for the interaction of GtCPES with the apophycobiliprotein CpeB is proposed and discussed.
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