Claudia Hackenberg, Johanna Hakanpaeae, Fei Cai, Svetlana Antonyuk, Caroline Eigner, Sven Meissner, Mikko Laitaoja, Janne Janis, Cheryl A. Kerfeld, Elke Dittmann, Victor S. Lamzin
- Cyanobacteria are important photosynthetic organisms inhabiting a range of dynamic environments. This phylum is distinctive among photosynthetic organisms in containing genes encoding uncharacterized cystathionine beta-synthase (CBS)-chloroplast protein (CP12) fusion proteins. These consist of two domains, each recognized as stand-alone photosynthetic regulators with different functions described in cyanobacteria (CP12) and plants (CP12 and CBSX). Here we show that CBS-CP12 fusion proteins are encoded in distinct gene neighborhoods, several unrelated to photosynthesis. Most frequently, CBS-CP12 genes are in a gene cluster with thioredoxin A (TrxA), which is prevalent in bloom-forming, marine symbiotic, and benthic mat cyanobacteria. Focusing on a CBS-CP12 from Microcystis aeruginosa PCC 7806 encoded in a gene cluster with TrxA, we reveal that the domain fusion led to the formation of a hexameric protein. We show that the CP12 domain is essential for hexamerization and contains an ordered, previously structurally uncharacterizedCyanobacteria are important photosynthetic organisms inhabiting a range of dynamic environments. This phylum is distinctive among photosynthetic organisms in containing genes encoding uncharacterized cystathionine beta-synthase (CBS)-chloroplast protein (CP12) fusion proteins. These consist of two domains, each recognized as stand-alone photosynthetic regulators with different functions described in cyanobacteria (CP12) and plants (CP12 and CBSX). Here we show that CBS-CP12 fusion proteins are encoded in distinct gene neighborhoods, several unrelated to photosynthesis. Most frequently, CBS-CP12 genes are in a gene cluster with thioredoxin A (TrxA), which is prevalent in bloom-forming, marine symbiotic, and benthic mat cyanobacteria. Focusing on a CBS-CP12 from Microcystis aeruginosa PCC 7806 encoded in a gene cluster with TrxA, we reveal that the domain fusion led to the formation of a hexameric protein. We show that the CP12 domain is essential for hexamerization and contains an ordered, previously structurally uncharacterized N-terminal region. We provide evidence that CBS-CP12, while combining properties of both regulatory domains, behaves different from CP12 and plant CBSX. It does not form a ternary complex with phosphoribulokinase (PRK) and glyceraldehyde-3-phosphate dehydrogenase. Instead, CBS-CP12 decreases the activity of PRK in an AMP-dependent manner. We propose that the novel domain architecture and oligomeric state of CBS-CP12 expand its regulatory function beyond those of CP12 in cyanobacteria.…
MetadatenAuthor details: | Claudia Hackenberg, Johanna Hakanpaeae, Fei Cai, Svetlana AntonyukORCiD, Caroline Eigner, Sven MeissnerGND, Mikko Laitaoja, Janne Janis, Cheryl A. KerfeldORCiD, Elke DittmannORCiDGND, Victor S. Lamzin |
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DOI: | https://doi.org/10.1073/pnas.1806668115 |
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ISSN: | 0027-8424 |
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Pubmed ID: | https://pubmed.ncbi.nlm.nih.gov/29915055 |
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Title of parent work (English): | Proceedings of the National Academy of Sciences of the United States of America |
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Publisher: | National Acad. of Sciences |
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Place of publishing: | Washington |
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Publication type: | Article |
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Language: | English |
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Date of first publication: | 2018/06/18 |
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Publication year: | 2018 |
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Release date: | 2021/11/02 |
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Tag: | Microcystis aeruginosa; crystal structure; hexamer; redox |
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Volume: | 115 |
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Issue: | 27 |
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Number of pages: | 6 |
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First page: | 7141 |
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Last Page: | 7146 |
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Funding institution: | EMBL; US Department of Energy, Basic Energy SciencesUnited States Department of Energy (DOE) [DE-FG02-91ER20021]; National Science FoundationNational Science Foundation (NSF) [IOS 1557324]; German Research Foundation (DFG)German Research Foundation (DFG) [Di910/10-1]; Erasmus scholarship; r Finland/Biocenter Kuopio; European Union Regional program [731077] |
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Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
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DDC classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
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Peer review: | Referiert |
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Publishing method: | Open Access / Hybrid Open-Access |
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License (German): | CC-BY-NC-ND - Namensnennung, nicht kommerziell, keine Bearbeitungen 4.0 International |
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