Submitted to: Photosynthesis Research
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 7/23/2008
Publication Date: 8/16/2008
Citation: Edelman, M., Mattoo, A.K. 2008. D1-protein dynamics in photosystem II: the lingering enigma. Photosynthesis Research. 98:609-620. Interpretive Summary: Life on earth was made possible with the evolution of oxygenic photosynthesis, which involves carbon dioxide fixation, and release of oxygen that we breathe. A major part of this process is initiated in chloroplasts by critical protein components associated with what is known as photosystem II. This photosystem is dominated by a protein called D1 which is one of the rapidly turning over proteins in plants and whose life history is tuned to light radiation. The D1 protein is possibly the most researched photosynthetic polypeptide. However, many aspects of its degradation and role of ligands that bind to it have, so far, defied clear resolution. We present data, arguments and concepts for rethinking of the data in literature and explain the cutting edge research with consequences on the mechanisms and possible function of D1 protein degradation. This research is important to biologists and biochemists involved with improvement of crop productivity through efficient photosynthesis.
Technical Abstract: The D1/D2 heterodimer core dominates the photosystem II reaction center. A characteristic feature of this heterodimer is the differentially rapid, light-dependent degradation of the D1 protein. The D1 protein is possibly the most researched photosynthetic polypeptide, with aspects of structure–function, gene, messenger and protein regulation, electron transport, reactive oxygen species, photoinhibition, herbicide binding, stromal–granal translocations, reversible phosphorylation and specific proteases all under intensive investigation more than three decades after the protein's debut in the literature. This review will touch on some treaded areas of D1 research that have, so far, defied clear resolution, as well as cutting edge research on mechanisms and consequences of D1 protein degradation.