The search for new chlorophyll-binding proteins in the cyanobacterium Synechocystis sp. PCC 6803

Otilia Cheregi, Willem Vermaas, Christiane Funk

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Light harvesting provides a major challenge in the production of biofuels from microorganisms; while sunlight provides the energy necessary for biomass/biofuel production, at the same time it damages the cells. The genome of Synechocystis sp. PCC 6803 was searched for open reading frames that might code for yet unidentified chlorophyll-binding proteins with low molecular mass that could be involved in stress-adaptation. Amongst 9167 hypothetical ORFs corresponding to potential polypeptides of 100 amino acids or less, two were identified that had the potential to be pigment-binding, because they (i) encoded a potential transmembrane region, (ii) showed sequence similarity with known chlorophyll-binding domains, (iii) were conserved in other cyanobacterial species, and (iv) their codon adaptation index indicated significant translation probability. The two ORFs were located complementary (antisense) and internal to the ferrochelatase (hemH) and the pyruvate dehydrogenase (pdh) genes and therefore were named a-fch and a-pdh, respectively. Transcription of both genes was confirmed; however, no translated proteins could be detected immunologically. Whereas mutations within a-pdh or a-fch did not lead to any obvious phenotype, it is clear that transcripts and proteins over and above the currently known set may play a role in defining the physiology of cyanobacteria and other organisms.

Original languageEnglish (US)
Pages (from-to)124-133
Number of pages10
JournalJournal of Biotechnology
Volume162
Issue number1
DOIs
StatePublished - Nov 30 2012

Fingerprint

Chlorophyll Binding Proteins
Synechocystis
Cyanobacteria
Chlorophyll
Pyruvic Acid
Open Reading Frames
Oxidoreductases
Biofuels
Genes
Ferrochelatase
Proteins
Sunlight
Polypeptides
Physiology
Molecular mass
Transcription
Pigments
Codon
Microorganisms
Membrane Potentials

Keywords

  • Antenna
  • Chlorophyll-binding protein
  • Light-harvesting
  • Non-photochemical quenching
  • Open reading frame
  • Synechocystis sp. PCC 6803

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

The search for new chlorophyll-binding proteins in the cyanobacterium Synechocystis sp. PCC 6803. / Cheregi, Otilia; Vermaas, Willem; Funk, Christiane.

In: Journal of Biotechnology, Vol. 162, No. 1, 30.11.2012, p. 124-133.

Research output: Contribution to journalArticle

@article{9e31cf6b34bc4382b31c42565f6425d5,
title = "The search for new chlorophyll-binding proteins in the cyanobacterium Synechocystis sp. PCC 6803",
abstract = "Light harvesting provides a major challenge in the production of biofuels from microorganisms; while sunlight provides the energy necessary for biomass/biofuel production, at the same time it damages the cells. The genome of Synechocystis sp. PCC 6803 was searched for open reading frames that might code for yet unidentified chlorophyll-binding proteins with low molecular mass that could be involved in stress-adaptation. Amongst 9167 hypothetical ORFs corresponding to potential polypeptides of 100 amino acids or less, two were identified that had the potential to be pigment-binding, because they (i) encoded a potential transmembrane region, (ii) showed sequence similarity with known chlorophyll-binding domains, (iii) were conserved in other cyanobacterial species, and (iv) their codon adaptation index indicated significant translation probability. The two ORFs were located complementary (antisense) and internal to the ferrochelatase (hemH) and the pyruvate dehydrogenase (pdh) genes and therefore were named a-fch and a-pdh, respectively. Transcription of both genes was confirmed; however, no translated proteins could be detected immunologically. Whereas mutations within a-pdh or a-fch did not lead to any obvious phenotype, it is clear that transcripts and proteins over and above the currently known set may play a role in defining the physiology of cyanobacteria and other organisms.",
keywords = "Antenna, Chlorophyll-binding protein, Light-harvesting, Non-photochemical quenching, Open reading frame, Synechocystis sp. PCC 6803",
author = "Otilia Cheregi and Willem Vermaas and Christiane Funk",
year = "2012",
month = "11",
day = "30",
doi = "10.1016/j.jbiotec.2012.06.022",
language = "English (US)",
volume = "162",
pages = "124--133",
journal = "Journal of Biotechnology",
issn = "0168-1656",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - The search for new chlorophyll-binding proteins in the cyanobacterium Synechocystis sp. PCC 6803

AU - Cheregi, Otilia

AU - Vermaas, Willem

AU - Funk, Christiane

PY - 2012/11/30

Y1 - 2012/11/30

N2 - Light harvesting provides a major challenge in the production of biofuels from microorganisms; while sunlight provides the energy necessary for biomass/biofuel production, at the same time it damages the cells. The genome of Synechocystis sp. PCC 6803 was searched for open reading frames that might code for yet unidentified chlorophyll-binding proteins with low molecular mass that could be involved in stress-adaptation. Amongst 9167 hypothetical ORFs corresponding to potential polypeptides of 100 amino acids or less, two were identified that had the potential to be pigment-binding, because they (i) encoded a potential transmembrane region, (ii) showed sequence similarity with known chlorophyll-binding domains, (iii) were conserved in other cyanobacterial species, and (iv) their codon adaptation index indicated significant translation probability. The two ORFs were located complementary (antisense) and internal to the ferrochelatase (hemH) and the pyruvate dehydrogenase (pdh) genes and therefore were named a-fch and a-pdh, respectively. Transcription of both genes was confirmed; however, no translated proteins could be detected immunologically. Whereas mutations within a-pdh or a-fch did not lead to any obvious phenotype, it is clear that transcripts and proteins over and above the currently known set may play a role in defining the physiology of cyanobacteria and other organisms.

AB - Light harvesting provides a major challenge in the production of biofuels from microorganisms; while sunlight provides the energy necessary for biomass/biofuel production, at the same time it damages the cells. The genome of Synechocystis sp. PCC 6803 was searched for open reading frames that might code for yet unidentified chlorophyll-binding proteins with low molecular mass that could be involved in stress-adaptation. Amongst 9167 hypothetical ORFs corresponding to potential polypeptides of 100 amino acids or less, two were identified that had the potential to be pigment-binding, because they (i) encoded a potential transmembrane region, (ii) showed sequence similarity with known chlorophyll-binding domains, (iii) were conserved in other cyanobacterial species, and (iv) their codon adaptation index indicated significant translation probability. The two ORFs were located complementary (antisense) and internal to the ferrochelatase (hemH) and the pyruvate dehydrogenase (pdh) genes and therefore were named a-fch and a-pdh, respectively. Transcription of both genes was confirmed; however, no translated proteins could be detected immunologically. Whereas mutations within a-pdh or a-fch did not lead to any obvious phenotype, it is clear that transcripts and proteins over and above the currently known set may play a role in defining the physiology of cyanobacteria and other organisms.

KW - Antenna

KW - Chlorophyll-binding protein

KW - Light-harvesting

KW - Non-photochemical quenching

KW - Open reading frame

KW - Synechocystis sp. PCC 6803

UR - http://www.scopus.com/inward/record.url?scp=84867648797&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84867648797&partnerID=8YFLogxK

U2 - 10.1016/j.jbiotec.2012.06.022

DO - 10.1016/j.jbiotec.2012.06.022

M3 - Article

VL - 162

SP - 124

EP - 133

JO - Journal of Biotechnology

JF - Journal of Biotechnology

SN - 0168-1656

IS - 1

ER -