TY - JOUR
T1 - Compartmentalization of the protein repair machinery in photosynthetic membranes
AU - Puthiyaveetil, Sujith
AU - Tsabari, Onie
AU - Lowry, Troy
AU - Lenhert, Steven
AU - Lewis, Robert R.
AU - Reich, Ziv
AU - Kirchhoff, Helmut
N1 - Washington State Agricultural Research Center; National Science Foundation [MCB-1158571]; United States-Israel Binational Agricultural Research and Development Fund [US-4334-10]; Israel Science Foundation [1034/12]; Human Frontier Science Program Organization [RGP0005/2013]We thank Dr. Dario Leister for providing curt1abcd quadruple mutant seeds and CURT1A antibody and Dr. Goldschmid-Clermont for the PBCP antibody. We thank Robert Yarbrough for proofreading the manuscript. This research was supported by the Washington State Agricultural Research Center, the National Science Foundation (Grant MCB-1158571), and the United States-Israel Binational Agricultural Research and Development Fund (Grant US-4334-10). Z.R. received funding from the Israel Science Foundation (Grant 1034/12) and the Human Frontier Science Program Organization (Grant RGP0005/2013).
PY - 2014/11/4
Y1 - 2014/11/4
N2 - A crucial component of protein homeostasis in cells is the repair of damaged proteins. The repair of oxygen-evolving photosystem II (PS II) supercomplexes in plant chloroplasts is a prime example of a very efficient repair process that evolved in response to the high vulnerability of PS II to photooxidative damage, exacerbated by high-light (HL) stress. Significant progress in recent years has unraveled individual components and steps that constitute the PS II repair machinery, which is embedded in the thylakoid membrane system inside chloroplasts. However, an open question is how a certain order of these repair steps is established and how unwanted back-reactions that jeopardize the repair efficiency are avoided. Here, we report that spatial separation of key enzymes involved in PS II repair is realized by subcompartmentalization of the thylakoid membrane, accomplished by the formation of stacked grana membranes. The spatial segregation of kinases, phosphatases, proteases, and ribosomes ensures a certain order of events with minimal mutual interference. The margins of the grana turn out to be the site of protein degradation, well separated from active PS II in grana core and de novo protein synthesis in unstacked stroma lamellae. Furthermore, HL induces a partial conversion of stacked grana core to grana margin, which leads to a controlled access of proteases to PS II. Our study suggests that the origin of grana in evolution ensures high repair efficiency, which is essential for PS II homeostasis.
AB - A crucial component of protein homeostasis in cells is the repair of damaged proteins. The repair of oxygen-evolving photosystem II (PS II) supercomplexes in plant chloroplasts is a prime example of a very efficient repair process that evolved in response to the high vulnerability of PS II to photooxidative damage, exacerbated by high-light (HL) stress. Significant progress in recent years has unraveled individual components and steps that constitute the PS II repair machinery, which is embedded in the thylakoid membrane system inside chloroplasts. However, an open question is how a certain order of these repair steps is established and how unwanted back-reactions that jeopardize the repair efficiency are avoided. Here, we report that spatial separation of key enzymes involved in PS II repair is realized by subcompartmentalization of the thylakoid membrane, accomplished by the formation of stacked grana membranes. The spatial segregation of kinases, phosphatases, proteases, and ribosomes ensures a certain order of events with minimal mutual interference. The margins of the grana turn out to be the site of protein degradation, well separated from active PS II in grana core and de novo protein synthesis in unstacked stroma lamellae. Furthermore, HL induces a partial conversion of stacked grana core to grana margin, which leads to a controlled access of proteases to PS II. Our study suggests that the origin of grana in evolution ensures high repair efficiency, which is essential for PS II homeostasis.
UR - http://www.scopus.com/inward/record.url?scp=84914680514&partnerID=8YFLogxK
U2 - https://doi.org/10.1073/pnas.1413739111
DO - https://doi.org/10.1073/pnas.1413739111
M3 - مقالة
SN - 0027-8424
VL - 111
SP - 15839
EP - 15844
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 44
ER -