Journal
PLANT SIGNALING & BEHAVIOR
Volume 8, Issue 2, Pages -Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/psb.22860
Keywords
Arabidopsis; chloroplast; envelope membrane; grana; osmotic stress; PspA; thylakoid biogenesis
Categories
Funding
- Japan Science and Technology Agency (Core Research for Evolutional Science and Technology, to W.S.)
- Oohara Foundation
Ask authors/readers for more resources
VIPP1 protein in photosynthetic organisms is homologous to bacterial PspA, which protects plasma membrane integrity upon stresses. Despite the proposed role of VIPP1 in thylakoid biogenesis, its precise function remains unclear. Recently, our in-depth analysis of Arabidopsis vipp1 mutants revealed VIPP1's involvement in the maintenance of chloroplast envelopes. Chloroplasts in intact vipp1 leaves exhibited spherical balloon-like morphology, which resulted from osmotic stress across envelopes. In fact, observation of VIPP1 fused to green fluorescence protein in vivo revealed that most VIPP1 is localized as a lattice-like macro complex attached along with the envelope. Because of the proposed function in thylakoids, we examined whether vipp1 also exhibited altered morphologies in thylakoids. Results show that thylakoid morphologies were detected irregularly, but vipp1 chloroplasts retained normal-appearing grana stacks. We infer that VIPP1 might influence thylakoids as well as envelopes, but that it is not involved
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available