dc.contributor.author | Skotnicová, Petra | |
dc.contributor.author | Srivastava, Amit | |
dc.contributor.author | Aggarwal, Divya | |
dc.contributor.author | Talbot, Jana | |
dc.contributor.author | Karlínová, Iva | |
dc.contributor.author | Moos, Martin | |
dc.contributor.author | Mareš, Jan | |
dc.contributor.author | Bučinská, Lenka | |
dc.contributor.author | Koník, Peter | |
dc.contributor.author | Šimek, Petr | |
dc.contributor.author | Tichý, Martin | |
dc.contributor.author | Sobotka, Roman | |
dc.date.accessioned | 2023-11-27T06:55:21Z | |
dc.date.available | 2023-11-27T06:55:21Z | |
dc.date.issued | 2024 | |
dc.identifier.citation | Skotnicová, 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.other | CONVID_194554088 | |
dc.identifier.uri | https://jyx.jyu.fi/handle/123456789/92091 | |
dc.description.abstract | Biogenesis 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.mimetype | application/pdf | |
dc.language.iso | eng | |
dc.publisher | Wiley | |
dc.relation.ispartofseries | New Phytologist | |
dc.rights | CC BY-NC-ND 4.0 | |
dc.subject.other | BtpA | |
dc.subject.other | cyanobacteria | |
dc.subject.other | glutamyl-tRNA reductase | |
dc.subject.other | Synechocystis sp. PCC6803 | |
dc.subject.other | tetrapyrrole biosynthesis | |
dc.title | A thylakoid biogenesis BtpA protein is required for the initial step of tetrapyrrole biosynthesis in cyanobacteria | |
dc.type | research article | |
dc.identifier.urn | URN:NBN:fi:jyu-202311278105 | |
dc.contributor.laitos | Bio- ja ympäristötieteiden laitos | fi |
dc.contributor.laitos | Department of Biological and Environmental Science | en |
dc.contributor.oppiaine | Nanoscience Center | fi |
dc.contributor.oppiaine | Nanoscience Center | en |
dc.type.uri | http://purl.org/eprint/type/JournalArticle | |
dc.type.coar | http://purl.org/coar/resource_type/c_2df8fbb1 | |
dc.description.reviewstatus | peerReviewed | |
dc.format.pagerange | 1236-1249 | |
dc.relation.issn | 0028-646X | |
dc.relation.numberinseries | 3 | |
dc.relation.volume | 241 | |
dc.type.version | publishedVersion | |
dc.rights.copyright | © 2023 The Authors. New Phytologist © 2023 New Phytologist Foundation | |
dc.rights.accesslevel | openAccess | fi |
dc.type.publication | article | |
dc.subject.yso | biosynteesi | |
dc.subject.yso | syanobakteerit | |
dc.format.content | fulltext | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p14405 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p3324 | |
dc.rights.url | https://creativecommons.org/licenses/by-nc-nd/4.0/ | |
dc.relation.doi | 10.1111/nph.19397 | |
jyx.fundinginformation | The 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.okm | A1 | |