Unknown

Dataset Information

0

A novel chloroplast super-complex consisting of the ATP synthase and photosystem I reaction center.


ABSTRACT: Several 'super-complexes' of individual hetero-oligomeric membrane protein complexes, whose function is to facilitate intra-membrane electron and proton transfer and harvesting of light energy, have been previously characterized in the mitochondrial cristae and chloroplast thylakoid membranes. We report the presence of an intra-membrane super-complex dominated by the ATP-synthase, photosystem I (PSI) reaction-center complex and the ferredoxin-NADP+ Reductase (FNR) in the thylakoid membrane. The presence of the super-complex has been documented by mass spectrometry, clear-native PAGE and Western Blot analyses. This is the first documented presence of ATP synthase in a super-complex with the PSI reaction-center located in the non-appressed stromal domain of the thylakoid membrane.

SUBMITTER: Bhaduri S 

PROVIDER: S-EPMC7444523 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature

altmetric image

Publications

A novel chloroplast super-complex consisting of the ATP synthase and photosystem I reaction center.

Bhaduri Satarupa S   Singh Sandeep K SK   Cohn Whitaker W   Hasan S Saif SS   Whitelegge Julian P JP   Cramer William A WA  

PloS one 20200820 8


Several 'super-complexes' of individual hetero-oligomeric membrane protein complexes, whose function is to facilitate intra-membrane electron and proton transfer and harvesting of light energy, have been previously characterized in the mitochondrial cristae and chloroplast thylakoid membranes. We report the presence of an intra-membrane super-complex dominated by the ATP-synthase, photosystem I (PSI) reaction-center complex and the ferredoxin-NADP+ Reductase (FNR) in the thylakoid membrane. The  ...[more]

Similar Datasets

2019-10-14 | PXD013406 | Pride
| S-EPMC5413553 | biostudies-literature
| S-EPMC6896225 | biostudies-literature
| S-EPMC3788808 | biostudies-literature
| S-EPMC7582616 | biostudies-literature
| S-EPMC7116070 | biostudies-literature
| S-EPMC7468127 | biostudies-literature
| S-EPMC41081 | biostudies-other
| S-EPMC3837435 | biostudies-literature
| S-EPMC4487076 | biostudies-literature