Characterization of the genes encoding phycoerythrin in the red alga Rhodella violacea : evidence for a splitting of the rpeB gene by an intron

Published on Oct 15, 1992in Proceedings of the National Academy of Sciences of the United States of America 9.50
· DOI :10.1073/pnas.89.20.9564
C Bernard1
Estimated H-index: 1
(Centre national de la recherche scientifique),
Jean-Claude Thomas20
Estimated H-index: 20
(Centre national de la recherche scientifique)
+ 4 AuthorsJ P Dubacq1
Estimated H-index: 1
(Centre national de la recherche scientifique)
Abstract
Abstract The phycobilisome of the eukaryotic unicellular red alga Rhodella violacea presents in some respects an organization that is intermediate between those of the homologous counterparts found in cyanobacteria (the putative chloroplast progenitor) and more advanced, pluricellular red algae. This suggests evolutionary relationships that we investigated at the genome level. The present work describes the sequences of two rhodophytan phycobilisome genes, rpeA and rpeB. These chloroplast genes encode the alpha and beta subunits of phycoerythrin, the major component of the light-harvesting antennae and one of the most abundant cellular proteins in these algae. The amino acid sequences deduced from both rpeA and rpeB present strong homologies with those previously reported for phycoerythrin subunits of cyanobacteria, rhodophyta, and cryptomonads. The main difference with the corresponding cyanobacterial genes was the unexpected occurrence of an intervening sequence that split rpeB into two exons. This intervening sequence presents characteristics of group II introns but lacks several structural domains. Transcriptional analyses showed that the two rpe genes are cotranscribed and that the major RNA species detected corresponds to a mature mRNA lacking the intron. As the phycobiliproteins form a group of closely related polypeptides in cyanobacteria and rhodophyta, the molecular events affecting the corresponding genes, such as the rpeB intron, may be a clue to elucidate some aspects of the molecular processes involved in the evolution of plastid genes.
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Cited By29
Wolfgang Löffelhardt23
Estimated H-index: 23
(University of Vienna),
Hans J. Bohnert75
Estimated H-index: 75
(University of Arizona)
Publisher Summary This chapter describes the importance of Cyanophora cyanelles for the comprehension of plastid evolution. It summarizes cyanelle biochemistry, wall structure, and genome organization. Cyanelles, like cyanobacteria, are surrounded by a peptidoglycan wall. In addition, cyanelles resemble cyanobacteria in their pigment composition and in possessing a carboxysome-like structure. Cyanophora cyanelles, especially in the stationary phase of growth, develop a characteristic protein inc...
12 Citations Source Cite
Published on Apr 1, 1994in FEBS Journal 4.53
Axel Ducret7
Estimated H-index: 7
,
Walter Sidler19
Estimated H-index: 19
+ 1 AuthorsHerbert Zuber39
Estimated H-index: 39
We present here the complete primary structure of R-phycocyanin-I α and β subunits from the red alga Porphyridium cruentum. The α chain is composed of 162 amino acid residues (18049Da, calculated from sequence, including chromophore) and carries a phycocyanobilin pigment covalently linked to Cys84. The β chain contains 172 amino acids (19344Da, calculated from sequence, including chromophores) and carries a phycocyanobilin pigment covalently linked at Cys82 and a phycoerythrobilin pigment at Cys...
27 Citations Source Cite
Published on Jan 1, 1993in Current Opinion in Genetics & Development 5.00
Michael W. Gray67
Estimated H-index: 67
(Dalhousie University)
Abstract Molecular data (particularly sequence analyses) have established that two eukaryotic organelles, the mitochondrion and the plastid, are the descendants of endosymbiotic (eu)bacteria whose closest living relatives are the α-Proteobacteria (mitochondrion) and Cyanobacteria (plastid). This review describes recent data that favor the view that each organelle arose via this primary endosymbiotic pathway only once (monophyletic origin), such as the discovery of group I introns that appear to ...
202 Citations Source Cite
Published on Oct 1, 1994in Plant Physiology 5.95
C. Bernard2
Estimated H-index: 2
,
N Tandeau de Marsac1
Estimated H-index: 1
,
Jean-Claude Thomas20
Estimated H-index: 20
3 Citations Source Cite
Published on Sep 1, 2011in Process Biochemistry 2.62
Asha Parmar9
Estimated H-index: 9
(Sardar Patel University),
Niraj Kumar Singh10
Estimated H-index: 10
(Sardar Patel University)
+ 1 AuthorsDatta Madamwar42
Estimated H-index: 42
(Sardar Patel University)
Abstract In this study, we describe a series of experiments presenting the biochemical evidence for the cleavage of an intact phycoerythrin (α and β subunits) to phycoerythrin with only fragmented α-subunit, which is also functional, in Phormidium sp. A27DM. Culture, whether grown in different conditions (static or sparging) or in medium with different pH, produced truncated phycoerythrin. This indicated that the growth conditions or pH of medium did not lead to cleavage of phycoerythrin. Cultur...
12 Citations Source Cite
Published on Dec 1, 1997in Phycological Research 1.27
Beom-Kyu Kim1
Estimated H-index: 1
,
Yuji Fujita14
Estimated H-index: 14
(Nagasaki University)
SUMMARY The genes encoding the α and β subunits of the phycoerythrin (PE) from the red algae Porphyra yezoensis Ueda and Porphyra tenera K jell man were isolated by PCR amplification. The PE u subunit gene was located downstream (+ 74bp) of the PE β sub-unit encoding gene. The PE amino acid sequences of P. yezoensis and P. tenera, as deduced from the nucleotide sequence of the cpeA and cpeB genes, were respectively, 83–89% and 84–87% identical to species in other red algal genera. They were also...
1 Citations Source Cite
Published on Jun 1, 2014in Indian journal of plant physiology
Devendra Kumar2
Estimated H-index: 2
(Indian Agricultural Research Institute),
Dolly Wattal Dhar10
Estimated H-index: 10
(Indian Agricultural Research Institute)
+ 2 AuthorsSuresh Walia18
Estimated H-index: 18
(Indian Agricultural Research Institute)
In this study a simple protocol was developed for purifying phycocyanin (PC) from Spirulina platensis (CCC540) by using ammonium sulphate precipitation, followed by a single step chromatography by using DEAE-Cellulose-11 and acetate buffer. Precipitation with 65 % ammonium sulphate resulted in 80 % recovery of phycocyanin with purity of 1.5 (A620/A280). Thro1ugh chromatography an 80 % recovery of phycocyanin with a purity of 4.5 (A620/A280) was achieved. In SDS_PAGE analysis, the purified PC sho...
32 Citations Source Cite
Published on Jan 1, 2011in Bioresource Technology 5.81
Asha Parmar9
Estimated H-index: 9
(Sardar Patel University),
Niraj Kumar Singh10
Estimated H-index: 10
(Sardar Patel University)
+ 2 AuthorsDatta Madamwar42
Estimated H-index: 42
(Sardar Patel University)
Abstract The present study is focused on purification, characterization and comparison of phycoerythrins from three different marine cyanobacterial cultures – Phormidium sp. A27DM, Lyngbya sp. A09DM and Halomicronema sp. A32DM. ‘Phycoerythrin’ was successfully purified and characterized. On SDS–PAGE, the PE purified from all three young cultures showed four bands – corresponding to α and β subunits of each of PE-I and PE-II. However, phycoerythrin purified after prolonged growth of Phormidium sp...
40 Citations Source Cite
Published on May 1, 2014in Journal of Plant Research 2.00
Naoyuki Tajima8
Estimated H-index: 8
(University of Tokyo),
Shusei Sato80
Estimated H-index: 80
(Tohoku University)
+ 6 AuthorsNaoki Sato39
Estimated H-index: 39
(University of Tokyo)
We determined the complete nucleotide sequence of the plastid genome of the unicellular marine red alga Porphyridium purpureum strain NIES 2140, belonging to the unsequenced class Porphyridiophyceae. The genome is a circular DNA composed of 217,694 bp with the GC content of 30.3 %. Twenty-nine of the 224 protein-coding genes contain one or multiple intron(s). A group I intron was found in the rpl28 gene, whereas the other introns were group II introns. The P. purpureum plastid genome has one non...
29 Citations Source Cite
Published on Apr 1, 1995in Journal of Molecular Biology 4.89
Kirk E. Apt8
Estimated H-index: 8
(Carnegie Institution for Science),
Jackie L. Collier20
Estimated H-index: 20
(Carnegie Institution for Science),
Arthur R. Grossman80
Estimated H-index: 80
(Carnegie Institution for Science)
Abstract Amino acid sequence alignments and phylogenetic analyses have been used to examine the relationships among 100 phycobiliprotein sequences. The alignments revealed a number of highly conserved amino acid residues that are involved in chromophore attachment and conformation, α-β interactions and phycobilisome assembly. The phylogenetic analysis confirmed that the phycobiliprotein subfamilies, previously classified by their biochemical and spectroscopic properties, also formed coherent evo...
177 Citations Source Cite
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