ArticleJournal of bacteriology2005
Two novel phycoerythrin-associated linker proteins in the marine cyanobacterium Synechococcus sp. strain WH8102.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 61 citations in OpenAlex.
- Competition for light color between marineApplied and environmental microbiology · 2025Article
- The structural basis for light acclimation in phycobilisome light harvesting systems systems in Porphyridium purpureum.Communications biology · 2023Article
- Dual thermal ecotypes coexist within a nearly genetically identical population of the unicellular marine cyanobacteriumProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Functional flexibility of cyanobacterial light harvesting phycobilisomes enable acclimation to the complex light regime of mixing marine water columns.The FEBS journal · 2023Article
- Chromatic Acclimation Processes and Their Relationships with Phycobiliprotein Complexes.Microorganisms · 2022Article
- Diversity and Evolution of Pigment Types in Marine Synechococcus Cyanobacteria.Genome biology and evolution · 2022Article
- The "Dark Side" of Picocyanobacteria: Life as We Do Not Know It (Yet).Microorganisms · 2022Review
- Comparative Thermophysiology of MarineFrontiers in microbiology · 2022Article
- MarineProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Assessment of the Allelochemical Activity and Biochemical Profile of Different Phenotypes of Picocyanobacteria from the GenusMarine drugs · 2020Article
- Insights Into the Evolution of Picocyanobacteria and Phycoerythrin Genes (Frontiers in microbiology · 2019Article
- A novel species of the marine cyanobacterium Acaryochloris with a unique pigment content and lifestyle.Scientific reports · 2018Article
- Evolution of the acceptor side of photosystem I: ferredoxin, flavodoxin, and ferredoxin-NADPPhotosynthesis research · 2017Review
- Adaptive thermostability of light-harvesting complexes in marine picocyanobacteria.The ISME journal · 2017Article
- Adaptation to Blue Light in MarineFrontiers in microbiology · 2017Article
- Phycobilisome: architecture of a light-harvesting supercomplex.Photosynthesis research · 2013Review
- Effect of temperature on photosynthesis and growth in marine Synechococcus spp.Plant physiology · 2013Article
- A gene island with two possible configurations is involved in chromatic acclimation in marine Synechococcus.PloS one · 2013Article
- Light history influences the response of the marine cyanobacterium Synechococcus sp. WH7803 to oxidative stress.Plant physiology · 2011Article
- Chromatic photoacclimation extends utilisable photosynthetically active radiation in the chlorophyll d-containing cyanobacterium, Acaryochloris marina.Photosynthesis research · 2009Article
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recent availability of the whole genome of Synechococcus sp. strain WH8102 allows us to have a global view of the complex structure of the phycobilisomes of this marine picocyanobacterium. Genomic analyses revealed several new characteristics of these phycobilisomes, consisting of an allophycocyanin core and rods made of one type of phycocyanin and two types of phycoerythrins (I and II). Although the allophycocyanin appears to be similar to that found commonly in freshwater cyanobacteria, the phycocyanin is simpler since it possesses only one complete set of alpha and beta subunits and two rod-core linkers (CpcG1 and CpcG2). It is therefore probably made of a single hexameric disk per rod. In contrast, we have found two novel putative phycoerythrin-associated linker polypeptides that appear to be specific for marine Synechococcus spp. The first one (SYNW2000) is unusually long (548 residues) and apparently results from the fusion of a paralog of MpeC, a phycoerythrin II linker, and of CpeD, a phycoerythrin-I linker. The second one (SYNW1989) has a more classical size (300 residues) and is also an MpeC paralog. A biochemical analysis revealed that, like MpeC, these two novel linkers were both chromophorylated with phycourobilin. Our data suggest that they are both associated (partly or totally) with phycoerythrin II, and we propose to name SYNW2000 and SYNW1989 MpeD and MpeE, respectively. We further show that acclimation of phycobilisomes to high light leads to a dramatic reduction of MpeC, whereas the two novel linkers are not significantly affected. Models for the organization of the rods are proposed.
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