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dc.contributor.authorSkotnicová, Petra
dc.contributor.authorSrivastava, Amit
dc.contributor.authorAggarwal, Divya
dc.contributor.authorTalbot, Jana
dc.contributor.authorKarlínová, Iva
dc.contributor.authorMoos, Martin
dc.contributor.authorMareš, Jan
dc.contributor.authorBučinská, Lenka
dc.contributor.authorKoník, Peter
dc.contributor.authorŠimek, Petr
dc.contributor.authorTichý, Martin
dc.contributor.authorSobotka, Roman
dc.date.accessioned2023-11-27T06:55:21Z
dc.date.available2023-11-27T06:55:21Z
dc.date.issued2024
dc.identifier.citationSkotnicová, P., Srivastava, A., Aggarwal, D., Talbot, J., Karlínová, I., Moos, M., Mareš, J., Bučinská, L., Koník, P., Šimek, P., Tichý, M., & Sobotka, R. (2024). A thylakoid biogenesis BtpA protein is required for the initial step of tetrapyrrole biosynthesis in cyanobacteria. <i>New Phytologist</i>, <i>241</i>(3), 1236-1249. <a href="https://doi.org/10.1111/nph.19397" target="_blank">https://doi.org/10.1111/nph.19397</a>
dc.identifier.otherCONVID_194554088
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/92091
dc.description.abstractBiogenesis of the photosynthetic apparatus requires complicated molecular machinery, individual components of which are either poorly characterized or unknown. The BtpA protein has been described as a factor required for the stability of photosystem I (PSI) in cyanobacteria; however, how the BtpA stabilized PSI remains unexplained. To clarify the role of BtpA, we constructed and characterized the btpA-null mutant (ΔbtpA) in the cyanobacterium Synechocystis sp. PCC 6803. The mutant contained only c. 1% of chlorophyll and nearly no thylakoid membranes. However, this strain, growing only in the presence of glucose, was genetically unstable and readily generated suppressor mutations that restore the photoautotrophy. Two suppressor mutations were mapped into the hemA gene encoding glutamyl-tRNA reductase (GluTR) – the first enzyme of tetrapyrrole biosynthesis. Indeed, the GluTR was not detectable in the ΔbtpA mutant and the suppressor mutations restored biosynthesis of tetrapyrroles and photoautotrophy by increased GluTR expression or by improved GluTR stability/processivity. We further demonstrated that GluTR associates with a large BtpA oligomer and that BtpA is required for the stability of GluTR. Our results show that the BtpA protein is involved in the biogenesis of photosystems at the level of regulation of tetrapyrrole biosynthesis.en
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherWiley
dc.relation.ispartofseriesNew Phytologist
dc.rightsCC BY-NC-ND 4.0
dc.subject.otherBtpA
dc.subject.othercyanobacteria
dc.subject.otherglutamyl-tRNA reductase
dc.subject.otherSynechocystis sp. PCC6803
dc.subject.othertetrapyrrole biosynthesis
dc.titleA thylakoid biogenesis BtpA protein is required for the initial step of tetrapyrrole biosynthesis in cyanobacteria
dc.typeresearch article
dc.identifier.urnURN:NBN:fi:jyu-202311278105
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineNanoscience Centeren
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.format.pagerange1236-1249
dc.relation.issn0028-646X
dc.relation.numberinseries3
dc.relation.volume241
dc.type.versionpublishedVersion
dc.rights.copyright© 2023 The Authors. New Phytologist © 2023 New Phytologist Foundation
dc.rights.accesslevelopenAccessfi
dc.type.publicationarticle
dc.subject.ysobiosynteesi
dc.subject.ysosyanobakteerit
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p14405
jyx.subject.urihttp://www.yso.fi/onto/yso/p3324
dc.rights.urlhttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.relation.doi10.1111/nph.19397
jyx.fundinginformationThe authors would like to thank Prof. Himadri Pakrasi (Washington University) for providing the original btpA mutant and the anti-BtpA antibody and to Prof. Ignacio Luque (University of Sevilla) for anti-glutamyl-tRNA synthetase antibody. This work was supported by the European Research Council Synergy Award 854126. RS would like to thank the Czech Science Foundation, grant no. 19-29225X, for the financial support. PK is supported by the Czech Ministry of Education, Youth and Sport, project CZ.02.1.01/0.0/0.0/15_003/0000441. Metabolomic (bioanalytical) analyses were supported by the Czech Science Foundation, project no. 23-06600S.
dc.type.okmA1


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