Unknown

Dataset Information

0

Plant and algal chlorophyll synthases function in Synechocystis and interact with the YidC/Alb3 membrane insertase.


ABSTRACT: In the model cyanobacterium Synechocystis sp. PCC 6803, the terminal enzyme of chlorophyll biosynthesis, chlorophyll synthase (ChlG), forms a complex with high light-inducible proteins, the photosystem II assembly factor Ycf39 and the YidC/Alb3/OxaI membrane insertase, co-ordinating chlorophyll delivery with cotranslational insertion of nascent photosystem polypeptides into the membrane. To gain insight into the ubiquity of this assembly complex in higher photosynthetic organisms, we produced functional foreign chlorophyll synthases in a cyanobacterial host. Synthesis of algal and plant chlorophyll synthases allowed deletion of the otherwise essential native cyanobacterial gene. Analysis of purified protein complexes shows that the interaction with YidC is maintained for both eukaryotic enzymes, indicating that a ChlG-YidC/Alb3 complex may be evolutionarily conserved in algae and plants.

SUBMITTER: Proctor MS 

PROVIDER: S-EPMC6175206 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Plant and algal chlorophyll synthases function in Synechocystis and interact with the YidC/Alb3 membrane insertase.

Proctor Matthew S MS   Chidgey Jack W JW   Shukla Mahendra K MK   Jackson Philip J PJ   Sobotka Roman R   Hunter C Neil CN   Hitchcock Andrew A  

FEBS letters 20180906 18


In the model cyanobacterium Synechocystis sp. PCC 6803, the terminal enzyme of chlorophyll biosynthesis, chlorophyll synthase (ChlG), forms a complex with high light-inducible proteins, the photosystem II assembly factor Ycf39 and the YidC/Alb3/OxaI membrane insertase, co-ordinating chlorophyll delivery with cotranslational insertion of nascent photosystem polypeptides into the membrane. To gain insight into the ubiquity of this assembly complex in higher photosynthetic organisms, we produced fu  ...[more]

Similar Datasets

| S-EPMC8733628 | biostudies-literature
| S-EPMC5675557 | biostudies-literature
| S-EPMC2820820 | biostudies-literature
| S-EPMC4463434 | biostudies-literature
| S-EPMC4124156 | biostudies-literature
| S-EPMC5766580 | biostudies-literature
| S-EPMC4252904 | biostudies-literature
| S-EPMC7886851 | biostudies-literature
| S-EPMC5048292 | biostudies-literature
| S-EPMC3602594 | biostudies-literature