Isolation and molecular characterization of rbcS in the unicellular green alga Nannochloris bacillaris (Chlorophyta, Trebouxiophyceae)

Tomokazu Yamazaki, Maki Yamamoto, Wataru Sakamoto, Shigeyuki Kawano

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The small subunit of the chloroplast enzyme ribulose-1,5-bisphosphate carboxyase/oxygenase (Rubisco) is encoded by rbcS. We isolated and characterized three rbcS genes (NbrbcS1-1, NbrbcS1-2, and NbrbcS2) from the unicellular green alga Nannochloris bacillaris (Chlorophyta, Trebouxiophyceae). In the haploid N. bacillaris genome, each is a single-copy gene located on different chromosomes. Each mature peptide contains 140 amino acid residues. NbrbcS1-1 and NbrbcS1-2 are identical and share 80% identity with NbrbcS2, while the respective transit sequences share only approximately 48% identity with that of NbrbcS2. NbrbcS1-1 transcription was suppressed in the dark and recovered drastically after transfer to light. In contrast, NbrbcS1-2 and NbrbcS2 expression 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 of NbrbcS1-1 and NbrbcS1-2 are identical to the corresponding introns of 37 rbcS genes in eight embryophyte species. While the second intron is conserved in the green algae, the NbrbcS2 intron appears to involve sliding by one base pair. The NbrbcS1-1 and NbrbcS1-2 intron conserved in green algae and embryophytes might be an ancestral intron from nuclear-encoded rbcS.

Original languageEnglish
Pages (from-to)67-76
Number of pages10
JournalPhycological Research
Volume53
Issue number1
DOIs
Publication statusPublished - Mar 2005

Fingerprint

Nannochloris
Chlorophyta
green alga
Introns
introns
chloroplast
peptide
protein
gene
Embryophyta
Chloroplasts
Green Fluorescent Proteins
tobacco
green fluorescent protein
sliding
chromosome
chloroplasts
genome
amino acid
peptides

Keywords

  • 5-bisphosphate carboxyase/ oxygenase (Rubisco)
  • Exon/ intron structure
  • Gene duplication
  • Gene transfer
  • Intron sliding
  • rbcS
  • Ribulose-1

ASJC Scopus subject areas

  • Plant Science
  • Microbiology
  • Oceanography

Cite this

Isolation and molecular characterization of rbcS in the unicellular green alga Nannochloris bacillaris (Chlorophyta, Trebouxiophyceae). / Yamazaki, Tomokazu; Yamamoto, Maki; Sakamoto, Wataru; Kawano, Shigeyuki.

In: Phycological Research, Vol. 53, No. 1, 03.2005, p. 67-76.

Research output: Contribution to journalArticle

@article{7b5377bee26a4d42aa528a120556e680,
title = "Isolation and molecular characterization of rbcS in the unicellular green alga Nannochloris bacillaris (Chlorophyta, Trebouxiophyceae)",
abstract = "The small subunit of the chloroplast enzyme ribulose-1,5-bisphosphate carboxyase/oxygenase (Rubisco) is encoded by rbcS. We isolated and characterized three rbcS genes (NbrbcS1-1, NbrbcS1-2, and NbrbcS2) from the unicellular green alga Nannochloris bacillaris (Chlorophyta, Trebouxiophyceae). In the haploid N. bacillaris genome, each is a single-copy gene located on different chromosomes. Each mature peptide contains 140 amino acid residues. NbrbcS1-1 and NbrbcS1-2 are identical and share 80{\%} identity with NbrbcS2, while the respective transit sequences share only approximately 48{\%} identity with that of NbrbcS2. NbrbcS1-1 transcription was suppressed in the dark and recovered drastically after transfer to light. In contrast, NbrbcS1-2 and NbrbcS2 expression 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 of NbrbcS1-1 and NbrbcS1-2 are identical to the corresponding introns of 37 rbcS genes in eight embryophyte species. While the second intron is conserved in the green algae, the NbrbcS2 intron appears to involve sliding by one base pair. The NbrbcS1-1 and NbrbcS1-2 intron conserved in green algae and embryophytes might be an ancestral intron from nuclear-encoded rbcS.",
keywords = "5-bisphosphate carboxyase/ oxygenase (Rubisco), Exon/ intron structure, Gene duplication, Gene transfer, Intron sliding, rbcS, Ribulose-1",
author = "Tomokazu Yamazaki and Maki Yamamoto and Wataru Sakamoto and Shigeyuki Kawano",
year = "2005",
month = "3",
doi = "10.1111/j.1440-183.2005.00374.x",
language = "English",
volume = "53",
pages = "67--76",
journal = "Phycological Research",
issn = "1322-0829",
publisher = "John Wiley and Sons Inc.",
number = "1",

}

TY - JOUR

T1 - Isolation and molecular characterization of rbcS in the unicellular green alga Nannochloris bacillaris (Chlorophyta, Trebouxiophyceae)

AU - Yamazaki, Tomokazu

AU - Yamamoto, Maki

AU - Sakamoto, Wataru

AU - Kawano, Shigeyuki

PY - 2005/3

Y1 - 2005/3

N2 - The small subunit of the chloroplast enzyme ribulose-1,5-bisphosphate carboxyase/oxygenase (Rubisco) is encoded by rbcS. We isolated and characterized three rbcS genes (NbrbcS1-1, NbrbcS1-2, and NbrbcS2) from the unicellular green alga Nannochloris bacillaris (Chlorophyta, Trebouxiophyceae). In the haploid N. bacillaris genome, each is a single-copy gene located on different chromosomes. Each mature peptide contains 140 amino acid residues. NbrbcS1-1 and NbrbcS1-2 are identical and share 80% identity with NbrbcS2, while the respective transit sequences share only approximately 48% identity with that of NbrbcS2. NbrbcS1-1 transcription was suppressed in the dark and recovered drastically after transfer to light. In contrast, NbrbcS1-2 and NbrbcS2 expression 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 of NbrbcS1-1 and NbrbcS1-2 are identical to the corresponding introns of 37 rbcS genes in eight embryophyte species. While the second intron is conserved in the green algae, the NbrbcS2 intron appears to involve sliding by one base pair. The NbrbcS1-1 and NbrbcS1-2 intron conserved in green algae and embryophytes might be an ancestral intron from nuclear-encoded rbcS.

AB - The small subunit of the chloroplast enzyme ribulose-1,5-bisphosphate carboxyase/oxygenase (Rubisco) is encoded by rbcS. We isolated and characterized three rbcS genes (NbrbcS1-1, NbrbcS1-2, and NbrbcS2) from the unicellular green alga Nannochloris bacillaris (Chlorophyta, Trebouxiophyceae). In the haploid N. bacillaris genome, each is a single-copy gene located on different chromosomes. Each mature peptide contains 140 amino acid residues. NbrbcS1-1 and NbrbcS1-2 are identical and share 80% identity with NbrbcS2, while the respective transit sequences share only approximately 48% identity with that of NbrbcS2. NbrbcS1-1 transcription was suppressed in the dark and recovered drastically after transfer to light. In contrast, NbrbcS1-2 and NbrbcS2 expression 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 of NbrbcS1-1 and NbrbcS1-2 are identical to the corresponding introns of 37 rbcS genes in eight embryophyte species. While the second intron is conserved in the green algae, the NbrbcS2 intron appears to involve sliding by one base pair. The NbrbcS1-1 and NbrbcS1-2 intron conserved in green algae and embryophytes might be an ancestral intron from nuclear-encoded rbcS.

KW - 5-bisphosphate carboxyase/ oxygenase (Rubisco)

KW - Exon/ intron structure

KW - Gene duplication

KW - Gene transfer

KW - Intron sliding

KW - rbcS

KW - Ribulose-1

UR - http://www.scopus.com/inward/record.url?scp=18144429133&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=18144429133&partnerID=8YFLogxK

U2 - 10.1111/j.1440-183.2005.00374.x

DO - 10.1111/j.1440-183.2005.00374.x

M3 - Article

AN - SCOPUS:18144429133

VL - 53

SP - 67

EP - 76

JO - Phycological Research

JF - Phycological Research

SN - 1322-0829

IS - 1

ER -