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dc.contributor.authorHackenberg, Claudia
dc.contributor.authorHakanpää, Johanna
dc.contributor.authorCai, Fei
dc.contributor.authorAntonyuk, Svetlana
dc.contributor.authorEigner, Caroline
dc.contributor.authorMeissner, Sven
dc.contributor.authorLaitaoja, Mikko
dc.contributor.authorJänis, Janne
dc.contributor.authorKerfeld, Cheryl A
dc.contributor.authorDittmann, Elke
dc.contributor.authorLamzin, Victor S
dc.date.accessioned2018-08-13T12:03:17Z
dc.date.available2018-08-13T12:03:17Z
dc.date.issued2018
dc.identifier.urihttps://erepo.uef.fi/handle/123456789/6780
dc.description.abstractCyanobacteria are important photosynthetic organisms inhabiting a range of dynamic environments. This phylum is distinctive among photosynthetic organisms in containing genes encoding uncharacterized cystathionine β-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.
dc.language.isoenglanti
dc.publisherProceedings of the National Academy of Sciences
dc.relation.ispartofseriesPROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
dc.relation.urihttp://dx.doi.org/10.1073/pnas.1806668115
dc.rightsCC BY-NC-ND https://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectcrystal structure
dc.subjecthexamer
dc.subjectredox
dc.subjectMicrocystis aeruginosa
dc.titleStructural and functional insights into the unique CBS-CP12 fusion protein family in cyanobacteria
dc.description.versionpublished version
dc.contributor.departmentDepartment of Chemistry, activities
uef.solecris.id55550132en
dc.type.publicationTieteelliset aikakauslehtiartikkelit
dc.rights.accessrights© Authors
dc.relation.doi10.1073/pnas.1806668115
dc.description.reviewstatuspeerReviewed
dc.format.pagerange7141-7146
dc.relation.issn0027-8424
dc.relation.issue27
dc.relation.volume115
dc.rights.accesslevelopenAccess
dc.type.okmA1
uef.solecris.openaccessHybridijulkaisukanavassa ilmestynyt avoin julkaisu


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