Thylakoid Localized Type 2 NAD(P)H Dehydrogenase NdbA Optimizes Light-Activated Heterotrophic Growth of Synechocystis sp. PCC 6803

dc.contributor.authorTuomas Huokko
dc.contributor.authorDorota Muth-Pawlak
dc.contributor.authorEva-Mari Aro
dc.contributor.organizationfi=molekulaarinen kasvibiologia|en=Molecular Plant Biology|
dc.contributor.organization-code1.2.246.10.2458963.20.50535969575
dc.converis.publication-id41684118
dc.converis.urlhttps://research.utu.fi/converis/portal/Publication/41684118
dc.date.accessioned2022-10-27T11:57:16Z
dc.date.available2022-10-27T11:57:16Z
dc.description.abstract<p>NdbA, one of the three type 2 NAD(P)H dehydrogenases (NDH-2) in <em>Synechocystis</em> sp. PCC 6803 (hereafter <em>Synechocystis</em>) was here localized to the thylakoid membrane (TM), unique for the three NDH-2s, and investigated with respect to photosynthetic and cellular redox metabolism. For this purpose, a deletion mutant (Δ<em>ndbA</em>) and a complementation strain overexpressing NdbA (Δ<em>ndbA</em>::<em>ndbA</em>) were constructed. It is demonstrated that NdbA is expressed at very low level in the wild-type (WT) <em>Synechocystis</em> under photoautotrophic (PA) growth whilst substantially higher expression occurs under light-activated heterotrophic growth (LAHG). The absence of NdbA resulted in non-optimal growth of <em>Synechocystis</em> under LAHG and concomitantly enhanced the expression of photoprotection-related flavodiiron proteins and carbon acquisition-related proteins as well as various transporters, but downregulated a few iron homeostasis-related proteins. NdbA overexpression, on the other hand, promoted photosynthetic pigmentation and functionality of photosystem I under LAHG conditions while distinct photoprotective and carbon concentrating proteins were downregulated. NdbA overexpression also exerted an effect on the expression of many signaling and gene regulation proteins. It is concluded that the amount and function of NdbA in the TM has a capacity to modulate the redox signaling of gene expression, but apparently has a major physiological role in maintaining iron homeostasis under LAHG conditions. LC-MS/MS data are available via ProteomeXchange with identifier PXD011671.</p>
dc.format.pagerange1386
dc.format.pagerange1399
dc.identifier.jour-issn0032-0781
dc.identifier.olddbid173069
dc.identifier.oldhandle10024/156163
dc.identifier.urihttps://www.utupub.fi/handle/11111/30923
dc.identifier.urnURN:NBN:fi-fe2021042822185
dc.language.isoen
dc.okm.affiliatedauthorHuokko, Tuomas
dc.okm.affiliatedauthorMuth-Pawlak, Dorota
dc.okm.affiliatedauthorAro, Eva-Mari
dc.okm.discipline1183 Plant biology, microbiology, virologyen_GB
dc.okm.discipline1183 Kasvibiologia, mikrobiologia, virologiafi_FI
dc.okm.internationalcopublicationnot an international co-publication
dc.okm.internationalityInternational publication
dc.okm.typeA1 ScientificArticle
dc.publisherNLM (Medline)
dc.publisher.countryUnited Kingdomen_GB
dc.publisher.countryBritanniafi_FI
dc.publisher.country-codeGB
dc.relation.doi10.1093/pcp/pcz044
dc.relation.ispartofjournalPlant and Cell Physiology
dc.relation.issue6
dc.relation.volume60
dc.source.identifierhttps://www.utupub.fi/handle/10024/156163
dc.titleThylakoid Localized Type 2 NAD(P)H Dehydrogenase NdbA Optimizes Light-Activated Heterotrophic Growth of Synechocystis sp. PCC 6803
dc.year.issued2019

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