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- Title
Isolation and molecular characterization ofrbcSin the unicellular green algaNannochloris bacillaris(Chlorophyta, Trebouxiophyceae).
- Authors
Yamazaki, Tomokazu; Yamamoto, Maki; Sakamoto, Wataru; Kawano, Shigeyuki
- Abstract
The small subunit of the chloroplast enzyme ribulose-1,5-bisphosphate carboxyase/oxygenase (Rubisco) is encoded byrbcS. We isolated and characterized threerbcSgenes (NbrbcS1-1,NbrbcS1-2, andNbrbcS2) from the unicellular green algaNannochloris bacillaris(Chlorophyta, Trebouxiophyceae). In the haploidN. bacillarisgenome, each is a single-copy gene located on different chromosomes. Each mature peptide contains 140 amino acid residues.NbrbcS1-1andNbrbcS1-2are identical and share 80% identity withNbrbcS2, while the respective transit sequences share only approximately 48% identity with that ofNbrbcS2.NbrbcS1-1transcription was suppressed in the dark and recovered drastically after transfer to light. In contrast,NbrbcS1-2andNbrbcS2expression were not reduced after transfer from light to dark. In chlorophyllic tobacco cells containing green fluorescent protein fusion proteins of the transit sequences of each peptide, green fluorescent protein signals were localized on particles matching chloroplasts. The first introns ofNbrbcS1-1andNbrbcS1-2are identical to the corresponding introns of 37rbcSgenes in eight embryophyte species. While the second intron is conserved in the green algae, theNbrbcS2intron appears to involve sliding by one base pair. TheNbrbcS1-1andNbrbcS1-2intron conserved in green algae and embryophytes might be an ancestral intron from nuclear-encodedrbcS.
- Subjects
GREEN algae; GREEN fluorescent protein; NONVASCULAR plants; AQUATIC resources; PHYTOPLANKTON; AMINO acids
- Publication
Phycological Research, 2005, Vol 53, Issue 1, p67
- ISSN
1322-0829
- Publication type
Article
- DOI
10.1111/j.1440-1835.2005.tb00358.x