RT Journal Article
SR Electronic
T1 Dynamical localization of a thylakoid membrane binding protein is required for acquisition of photosynthetic competency
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 199943
DO 10.1101/199943
A1 Andrian Gutu
A1 Frederick Chang
A1 Erin K. O‘Shea
YR 2017
UL http://biorxiv.org/content/early/2017/10/08/199943.abstract
AB Vipp1 is highly conserved and essential for photosynthesis, but its function is unclear as it does not participate directly in light-dependent reactions. We analyzed Vipp1 localization in live cyanobacterial cells and show that Vipp1 is highly dynamic, continuously exchanging between a diffuse fraction that is uniformly distributed throughout the cell and a punctate fraction that is concentrated at high curvature regions of the thylakoid located at the cell periphery. Experimentally perturbing the spatial distribution of Vipp1 by relocalizing it to the nucleoid causes a severe growth defect during the transition from non-photosynthetic (dark) to photosynthetic (light) growth. However, the same perturbation of Vipp1 in dark alone or light alone growth conditions causes no growth or thylakoid morphology defects. We propose that the punctuated dynamics of Vipp1 at the cell periphery in regions of high thylakoid curvature enable acquisition of photosynthetic competency, perhaps by facilitating biogenesis of photosynthetic complexes involved in light-dependent reactions of photosynthesis.