Small Cab-like proteins regulating tetrapyrrole biosynthesis in the cyanobacterium Synechocystis sp. Pcc 6803

Hong Xu, Dmitrii Vavilin, Christiane Funk, Willem Vermaas

Research output: Contribution to journalArticle

69 Citations (Scopus)

Abstract

In the cyanobacterium Synechocystis sp. PCC 6803 five open reading frames (scpA-scpE) have been identified that code for single-helix proteins resembling helices I and III of chlorophyll a/b-binding (Cab) antenna proteins from higher plants. They have been named SCPs (small Cab-like proteins). Deletion of a single scp gene in a wild-type or in a photosystem I-less (PS I-less) strain has little effect. However, the effects of functional deletion of scpB or scpE were remarkable under conditions where chlorophyll availability was limited. When cells of a strain lacking PS I and chlL (coding for a polypeptide needed for light-independent protochlorophyllide reduction) were grown in darkness, the phycobilin and protochlorophyllide levels decreased upon deletion of scpB or scpE and the protoheme level was reduced in the strain lacking scpE. Addition of δ-aminolevulinic acid (ALA) in darkness drastically increased the level of Mg-protoporphyrin IX and Mg-protoporphyrin 1X monomethyl ester in the PS 1-less/chlL-/scpE- strain, whereas PChlide accumulated in the PS I-less/chIL-/scpB- strain. In the PS I-less/chlL- control strain ALA supplementation did not lead to large changes in the levels of tetrapyrrole biosynthesis intermediates. We propose that ScpE and ScpB regulate tetrapyrrole biosynthesis as a function of pigment availability. This regulation occurs primarily at an early step of tetrapyrrole biosynthesis, prior to ALA. In view of the conserved nature of chlorophyll-binding sites in these proteins, it seems likely that regulation by SCPs occurs as a function of chlorophyll availability, with SCPs activating chlorophyll biosynthesis steps when they do not have pigments bound.

Original languageEnglish (US)
Pages (from-to)149-160
Number of pages12
JournalPlant Molecular Biology
Volume49
Issue number2
DOIs
StatePublished - 2002

Fingerprint

Tetrapyrroles
Chlorophyll Binding Proteins
Synechocystis
Biosynthesis
Cyanobacteria
Chlorophyll
Photosystem I Protein Complex
Aminolevulinic Acid
Protochlorophyllide
biosynthesis
chlorophyll
Darkness
aminolevulinic acid
Phycobilins
photosystem I
Proteins
proteins
Availability
protochlorophyllides
Pigments

Keywords

  • Chlorophyll biosynthesis
  • Cyanobacteria
  • Feedback regulation
  • Small Cab-like proteins
  • Tetrapyrrole biosynthesis pathway

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Small Cab-like proteins regulating tetrapyrrole biosynthesis in the cyanobacterium Synechocystis sp. Pcc 6803. / Xu, Hong; Vavilin, Dmitrii; Funk, Christiane; Vermaas, Willem.

In: Plant Molecular Biology, Vol. 49, No. 2, 2002, p. 149-160.

Research output: Contribution to journalArticle

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AB - In the cyanobacterium Synechocystis sp. PCC 6803 five open reading frames (scpA-scpE) have been identified that code for single-helix proteins resembling helices I and III of chlorophyll a/b-binding (Cab) antenna proteins from higher plants. They have been named SCPs (small Cab-like proteins). Deletion of a single scp gene in a wild-type or in a photosystem I-less (PS I-less) strain has little effect. However, the effects of functional deletion of scpB or scpE were remarkable under conditions where chlorophyll availability was limited. When cells of a strain lacking PS I and chlL (coding for a polypeptide needed for light-independent protochlorophyllide reduction) were grown in darkness, the phycobilin and protochlorophyllide levels decreased upon deletion of scpB or scpE and the protoheme level was reduced in the strain lacking scpE. Addition of δ-aminolevulinic acid (ALA) in darkness drastically increased the level of Mg-protoporphyrin IX and Mg-protoporphyrin 1X monomethyl ester in the PS 1-less/chlL-/scpE- strain, whereas PChlide accumulated in the PS I-less/chIL-/scpB- strain. In the PS I-less/chlL- control strain ALA supplementation did not lead to large changes in the levels of tetrapyrrole biosynthesis intermediates. We propose that ScpE and ScpB regulate tetrapyrrole biosynthesis as a function of pigment availability. This regulation occurs primarily at an early step of tetrapyrrole biosynthesis, prior to ALA. In view of the conserved nature of chlorophyll-binding sites in these proteins, it seems likely that regulation by SCPs occurs as a function of chlorophyll availability, with SCPs activating chlorophyll biosynthesis steps when they do not have pigments bound.

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