Unknown

Dataset Information

0

Attachment of Ferredoxin: NADP+ Oxidoreductase to Phycobilisomes Is Required for Photoheterotrophic Growth of the Cyanobacterium Synechococcus sp. PCC 7002.


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.

SUBMITTER: Li X 

PROVIDER: S-EPMC9319322 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC3067432 | biostudies-literature
| S-EPMC4309022 | biostudies-literature
| S-EPMC103701 | biostudies-literature
| S-EPMC4628125 | biostudies-literature
| S-EPMC7406221 | biostudies-literature
| S-EPMC4851311 | biostudies-literature
| S-EPMC4431953 | biostudies-literature
| S-EPMC7880944 | biostudies-literature
| S-EPMC6950573 | biostudies-literature
| S-EPMC6361979 | biostudies-literature