A1 Refereed original research article in a scientific journal
Thylakoid Localized Type 2 NAD(P)H Dehydrogenase NdbA Optimizes Light-Activated Heterotrophic Growth of Synechocystis sp. PCC 6803
Authors: Tuomas Huokko, Dorota Muth-Pawlak, Eva-Mari Aro
Publisher: NLM (Medline)
Publication year: 2019
Journal:Plant and Cell Physiology
Journal name in sourcePlant & cell physiology
Volume: 60
Issue: 6
First page : 1386
Last page: 1399
Number of pages: 14
ISSN: 1471-9053
DOI: https://doi.org/10.1093/pcp/pcz044
Self-archived copy’s web address: https://research.utu.fi/converis/portal/detail/Publication/41684118
NdbA, one of the three type 2 NAD(P)H dehydrogenases (NDH-2) in Synechocystis sp. PCC 6803 (hereafter Synechocystis)
 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 (ΔndbA) and a complementation strain overexpressing NdbA (ΔndbA::ndbA) were constructed. It is demonstrated that NdbA is expressed at very low level in the wild-type (WT) Synechocystis
 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 Synechocystis
 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.
| Downloadable publication  This is an electronic reprint of the original article. | 

