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Identification of an Atypical Membrane Protein Involved in the Formation of Protein Disulfide Bonds in Oxygenic Photosynthetic Organisms
Open accessAbstract
The evolution of oxygenic photosynthesis in cyanobacteria nearly three billion years ago provided abundant reducing power and facilitated the elaboration of numerous oxygen-dependent reactions in our biosphere. Cyanobacteria contain an internal thylakoid membrane system, the site of photosynthesis, and a typical Gram-negative envelope membrane system. Like other organisms, the extracytoplasmic space in cyanobacteria houses numerous cysteine-containing proteins. However, the existence of a biochemical system for disulfide bond formation in cyanobacteria remains to be determined. Extracytoplasmic disulfide bond formation in non-photosynthetic organisms is catalyzed by coordinated interaction between two proteins, a disulfide carrier and a disulfide generator. Here we describe a novel gene, SyndsbAB, required for disulfide bond formation in the extracytoplasmic space of cyanobacteria. The SynDsbAB orthologs are present in most cyanobacteria and chloroplasts of higher plants with fully sequenced genomes. The SynDsbAB protein contains two distinct catalytic domains that display significant similarity to proteins involved in disulfide bond formation in Escherichia coli and eukaryotes. Importantly, SyndsbAB complements E. coli strains defective in disulfide bond formation. In addition, the activity of E. coli alkaline phosphatase localized to the periplasm of Synechocystis 6803 is dependent on the function of SynDsbAB. Deletion of SyndsbAB in Synechocystis 6803 causes significant growth impairment under photoautotrophic conditions and results in hyper-sensitivity to dithiothreitol, a reductant, whereas diamide, an oxidant had no effect on the growth of the mutant strains. We conclude that SynDsbAB is a critical protein for disulfide bond formation in oxygenic photosynthetic organisms and required for their optimal photoautotrophic growth.
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The cyanobacterial SynDsbAB system has been shown to support extracytoplasmic disulfide-bond formation in oxygenic photosynthetic organisms, highlighting the importance of redox-compatible localisation for disulfide-containing proteins.
“The cyanobacterial SynDsbAB system has been shown to support extracytoplasmic disulfide-bond formation in oxygenic photosynthetic organisms, highlighting the importance of redox-compatible localisation for disulfide-containing proteins [109].”
From Cyanobacteria as a Photosynthetic Chassis for Metabolic Pathway Engineering with Heterologous Gene Expression (2026) · cites this paper as [109]
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“The cyanobacterial SynDsbAB system has been shown to support extracytoplasmic disulfide-bond formation in oxygenic photosynthetic organisms, highlighting the importance of redox-compatible localisation for disulfide-containing proteins [109].”
Metadata
- Authors
- Singh, A. K., Bhattacharyya-Pakrasi, M., & Pakrasi, H. B.
- Affiliations
- Washington University in St. Louis (US)
- Corresponding author
- Pakrasi, Himadri B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-06
- Volume
- 283
- Issue
- 23
- Pages
- 15762-15770
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3259654
- OpenAlex
- W1980516267
- Cited by
- 73
- References
- 35
- Citations by year
- 2026: 5 · 2025: 1 · 2023: 1 · 2021: 1 · 2020: 2 · 2019: 2 · 2018: 4 · 2017: 5 · 2016: 2 · 2015: 5 · 2014: 4 · 2013: 6 · 2012: 5
- FWCI
- 4.11
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Keywords
- disulfide bond formation, cyanobacteria, Synechocystis sp. PCC 6803, membrane proteins, oxygenic photosynthesis, photoautotrophic growth, dithiothreitol sensitivity, alkaline phosphatase, periplasm, chloroplasts, evolution of photosynthesis
- MeSH terms
- Bacterial Proteins, Disulfides, Escherichia coli, Membrane Proteins, Photosynthesis, Synechocystis
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