ArticlePlant molecular biology1999
Phycoerythrins of the oxyphotobacterium Prochlorococcus marinus are associated to the thylakoid membrane and are encoded by a single large gene cluster.
Article in Plant molecular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 59 citations in OpenAlex.
- Article
- Phycobilisomes and Phycobiliproteins in the Pigment Apparatus of Oxygenic Photosynthetics: From Cyanobacteria to Tertiary Endosymbiosis.International journal of molecular sciences · 2023Review
- A novel species of the marine cyanobacterium Acaryochloris with a unique pigment content and lifestyle.Scientific reports · 2018Article
- Shedding new light on viral photosynthesis.Photosynthesis research · 2015Review
- Connecting thermal physiology and latitudinal niche partitioning in marine Synechococcus.The ISME journal · 2014Article
- The chloroplast proteome: a survey from the Chlamydomonas reinhardtii perspective with a focus on distinctive features.Current genetics · 2011Review
- Ecological genomics of marine picocyanobacteria.Microbiology and molecular biology reviews : MMBR · 2009Review
- Biliprotein maturation: the chromophore attachment.Molecular microbiology · 2008Review
- Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a nearly minimal oxyphototrophic genome.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Expression and phylogeny of the multiple antenna genes of the low-light-adapted strain Prochlorococcus marinus SS120 (Oxyphotobacteria).Plant molecular biology · 2001Article
- Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms.The Plant cell · 2001Article
- Diel expression of cell cycle-related genes in synchronized cultures of Prochlorococcus sp. strain PCC 9511.Journal of bacteriology · 2001Article
- The photosynthetic apparatus of Prochlorococcus: Insights through comparative genomics.Photosynthesis research · 2001Article
- Rapid evolutionary divergence of Photosystem I core subunits PsaA and PsaB in the marine prokaryote Prochlorococcus.Photosynthesis research · 2000Article
- Prochlorococcus, a marine photosynthetic prokaryote of global significance.Microbiology and molecular biology reviews : MMBR · 1999Review
- 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
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An intrinsic divinyl-chlorophyll a/b antenna and a particular form of phycobiliprotein, phycoerythrin (PE) III, coexist in the marine oxyphotobacterium Prochlorococcus marinus CCMP 1375. The genomic region including the cpeB/A operon of P. marinus was analysed. It encompasses 10,153 nucleotides that encode three structural phycobiliproteins and at least three (possibly five) different polypeptides analogous to cyanobacterial or red algal proteins involved either in the linkage of subunits or the synthesis and attachment of chromophoric groups. This gene cluster is part of the chromosome and is located within a distance of less than 110 kb from a previously characterized region containing the genes aspA-psbA-aroC. Whereas the Prochlorococcus phycobiliproteins are characterized by distinct deletions and amino acid replacements with regard to analogous proteins from other organisms, the gene arrangement resembles the organization of phycobiliprotein genes in some other cyanobacteria, in particular marine Synechococcus strains. The expression of two of the Prochlorococcus polypeptides as recombinant proteins in Escherichia coli allowed the production of individual homologous antisera to the Prochlorococcus alpha and beta PE subunits. Experiments using these sera show that the Prochlorococcus PEs are specifically associated to the thylakoid membrane and that the protein level does not significantly vary as a function of light irradiance or growth phase.
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