ArticlePhotosynthesis research1995
Cryptomonad biliproteins - an evolutionary perspective.
Article in Photosynthesis research, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 96 citations in OpenAlex.
- A Protein-Centric Mass Spectrometry Approach for Species Identification within Harmful Algal Blooms.Journal of the American Chemical Society · 2025Article
- The structural basis for light harvesting in organisms producing phycobiliproteins.The Plant cell · 2024Review
- Molecular dissection of the soluble photosynthetic antenna from the cryptophyte alga Hemiselmis andersenii.Communications biology · 2023Article
- Genomic insights into the coupling of a Chlorella-like microeukaryote and sulfur bacteria in the chemocline of permanently stratified Lake Cadagno.The ISME journal · 2023Article
- Infrared Signatures of Phycobilins within the Phycocyanin 645 Complex.The journal of physical chemistry. B · 2023Article
- Molecular structures reveal the origin of spectral variation in cryptophyte light harvesting antenna proteins.Protein science : a publication of the Protein Society · 2023Article
- Phycobilisomes and Phycobiliproteins in the Pigment Apparatus of Oxygenic Photosynthetics: From Cyanobacteria to Tertiary Endosymbiosis.International journal of molecular sciences · 2023Review
- Article
- Spectroscopic and Photophysical Investigation of Model Dipyrroles Common to Bilins: Exploring Natural Design for Steering Torsion to Divergent Functions.Frontiers in chemistry · 2021Article
- Estimation of the relative contributions to the electronic energy transfer rates based on Förster theory: The case of C-phycocyanin chromophores.Biophysics and physicobiology · 2021Article
- Diversification of light capture ability was accompanied by the evolution of phycobiliproteins in cryptophyte algae.Proceedings. Biological sciences · 2019Article
- Proteomic analysis of the phycobiliprotein antenna of the cryptophyte alga Guillardia theta cultured under different light intensities.Photosynthesis research · 2018Article
- Synthesis of chlorophyll-c derivatives by modifying natural chlorophyll-a.Photosynthesis research · 2016Article
- Chromophore composition of the phycobiliprotein Cr-PC577 from the cryptophyte Hemiselmis pacifica.Photosynthesis research · 2014Article
- Insights into the biosynthesis and assembly of cryptophycean phycobiliproteins.The Journal of biological chemistry · 2014Article
- Involvement of mammalian bilitranslocase-like protein(s) in chlorophyll catabolism of Pisum sativum L. tissues.Journal of bioenergetics and biomembranes · 2014Article
- CyanoLyase: a database of phycobilin lyase sequences, motifs and functions.Nucleic acids research · 2013Article
- Flow of excitation energy in the cryptophyte light-harvesting antenna phycocyanin 645.Biophysical journal · 2011Article
- The supramolecular architecture, function, and regulation of thylakoid membranes in red algae: an overview.Photosynthesis research · 2010Review
- Multiple independent losses of photosynthesis and differing evolutionary rates in the genus Cryptomonas (Cryptophyceae): combined phylogenetic analyses of DNA sequences of the nuclear and the nucleomorph ribosomal operons.Journal of molecular evolution · 2005Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Each cryptomonad strain contains only a single spectroscopic type of biliprotein. These biliproteins are isolated as ≈50000 kDa αα'β2 complexes which carry one bilin on the α and three on the β subunit. Six different bilins are present on the cryptomonad biliproteins, two of which (phycocyanobilin and phycoerythrobilin) also occur in cyanobacterial and rhodophytan biliproteins, while four are known only in the cryptomonads. The β subunit is encoded on the chloroplast genome, whereas the α subunits are encoded by a small nuclear multigene family. The β subunits of all cryptomonad biliproteins, regardless of spectroscopic type, have highly conserved amino acid sequences, which show > 80% identity with those of rhodophytan phycoerythrin β subunits. In contrast, cyanobacteria and red algal chloroplasts each contain several spectroscopically distinct biliproteins organized into macromolecular complexes (phycobilisomes). The data on biliproteins, as well as several other lines of evidence, indicate that the cryptomonad biliprotein antenna system is 'primitive' and antedates that of the cyanobacteria. It is proposed that the gene encoding the cryptomonad biliprotein β subunit is the ancestral gene of the gene family encoding cyanobacterial and rhodophytan biliprotein α and β subunits.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.