6533b85cfe1ef96bd12bd30e

RESEARCH PRODUCT

GreenCut proteinCPLD49 ofChlamydomonas reinhardtiiassociates with thylakoid membranes and is required for cytochromeb6fcomplex accumulation

Graham PeersKrishna K. NiyogiKrishna K. NiyogiWenqiang YangTyler M. WittkoppTyler M. WittkoppXenie JohnsonArthur R. GrossmanMark L. HeinnickelRick G. KimRick G. KimShai SaroussiWitchukorn PhuthongFrancis-andré WollmanRachel M. DentRachel M. DentJames J. RussellCorey D. BroecklingMartin Lohr

subject

0106 biological sciences0301 basic medicineCytochrome b6f complex[SDV]Life Sciences [q-bio]MutantChlamydomonas reinhardtii[SDV.BC]Life Sciences [q-bio]/Cellular BiologyCell BiologyPlant ScienceBiologyPhotosynthesisbiology.organism_classification01 natural sciencesElectron transport chainCell biologyChloroplast03 medical and health sciences030104 developmental biologyMembrane protein complexThylakoidGeneticsComputingMilieux_MISCELLANEOUS010606 plant biology & botany

description

The GreenCut encompasses a suite of nucleus-encoded proteins with orthologs among green lineage organisms (plants, green algae), but that are absent or poorly conserved in non-photosynthetic/heterotrophic organisms. In Chlamydomonas reinhardtii, CPLD49 (Conserved in Plant Lineage and Diatoms49) is an uncharacterized GreenCut protein that is critical for maintaining normal photosynthetic function. We demonstrate that a cpld49 mutant has impaired photoautotrophic growth under high-light conditions. The mutant exhibits a nearly 90% reduction in the level of the cytochrome b6 f complex (Cytb6 f), which impacts linear and cyclic electron transport, but does not compromise the ability of the strain to perform state transitions. Furthermore, CPLD49 strongly associates with thylakoid membranes where it may be part of a membrane protein complex with another GreenCut protein, CPLD38; a mutant null for CPLD38 also impacts Cytb6 f complex accumulation. We investigated several potential functions of CPLD49, with some suggested by protein homology. Our findings are congruent with the hypothesis that CPLD38 and CPLD49 are part of a novel thylakoid membrane complex that primarily modulates accumulation, but also impacts the activity of the Cytb6 f complex. Based on motifs of CPLD49 and the activities of other CPLD49-like proteins, we suggest a role for this putative dehydrogenase in the synthesis of a lipophilic thylakoid membrane molecule or cofactor that influences the assembly and activity of Cytb6 f.

https://doi.org/10.1111/tpj.13915