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- Title
Attachment of Ferredoxin: NADP + Oxidoreductase to Phycobilisomes Is Required for Photoheterotrophic Growth of the Cyanobacterium Synechococcus sp. PCC 7002.
- Authors
Li, Xiying; Huang, Chenhui; Wei, Peijun; Zhang, Kun; Dong, Chunxia; Lan, Qing; Zheng, Zhenggao; Zhang, Zhengdong; Zhao, Jindong
- Abstract
Two types of cyanobacterial phycobilisomes (PBS) are present: the hemidiscoidal PBS (CpcG-PBS) and the membrane-bound PBS (CpcL-PBS). Both types of PBS have ferredoxin:NADP+ oxidoreductase (FNR) attached to the termini of their rods through a CpcD domain. To date, the physiological significance of the attachment remains unknown. We constructed a mutant (dF338) which contains an FNR lacking the N-terminal CpcD domain in Synechococcus sp. PCC 7002. Isolated CpcG-PBS from dF338 did not contain FNR and the cell extracts of the mutant had a 35 kDa protein cross-reacting to anti-FNR antibodies. dF338 grows normally under photoautotrophic conditions, but little growth was observed under photoheterotrophic conditions. A cpcL (cpcG2) mutant grows extremely slowly under photoheterotrophic conditions while a cpcG (cpcG1) mutant, in which PBS rods could not attach to the cores of the CpcG-PBS, can grow photoheterotrophically, strongly suggesting that the attachment of FNR to CpcL-PBS is critical to photoheterotrophic growth. We show that electron transfer to the plastoquinone pool in dF338 and the cpcL mutant was impaired. We also provide evidence that trimeric photosystem I (PSI) and intact CpcL-PBS with a full-length FNR is critical to plastoquinone reduction. The presence of a NADPH-dehydrogenase (NDH)-CpcL-PBS-PSI trimer supercomplex and its roles are discussed.
- Subjects
PHYCOBILISOMES; SYNECHOCOCCUS; NICOTINAMIDE adenine dinucleotide phosphate; PHOTOSYSTEMS; CHARGE exchange; CYANOBACTERIAL toxins; FERREDOXINS
- Publication
Microorganisms, 2022, Vol 10, Issue 7, pN.PAG
- ISSN
2076-2607
- Publication type
Article
- DOI
10.3390/microorganisms10071313