|
|
||||||||
|
Plant Physiology Preview Published on May 26, 2006; 10.1104/pp.106.079046
Received February 9, 2006 A conserved mechanism controls translation of Rubisco large subunit in different photosynthetic organisms
Department of Life Sciences, Ben-Gurion University of the Negev, POBox 653, Beer-Sheva 84105, Israel * Corresponding author; email: shapiram{at}bgu.ac.il.
We previously proposed a novel mechanism for control of ribulose-1,5 biphosphate carboxylase/oxygenase (Rubisco) expression and assembly during oxidative stress in Chlamydomonas reinhardtii. The N-terminus of the large subunit (LSU) comprises an RNA recognition motif (RRM) that is normally buried in the protein, but becomes exposed under oxidizing conditions, when the glutathione pool shifts towards its oxidized form. Thus, de-novo translation and assembly of Rubisco LSU stop with similar kinetics, and the unpaired small subunit (SSU) is rapidly degraded. Here we show that the structure of the N-terminal domain is highly conserved throughout evolution, despite its relatively low sequence similarity. Furthermore, Rubisco from a broad evolutionary range of photosynthetic organisms binds RNA under oxidizing conditions, with Kd values in the nano-molar range. In line with these observations, oxidative stress indeed causes a translational arrest in land plants as well as in Rhodospirillum rubrum, a purple bacterium that lacks the SSU. We highlight an evolutionary conserved element located within
This article has been cited by other articles:
|
|||||||||||||||||||||||||||||||||||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| ASPB Publications | PLANT PHYSIOLOGY® | THE PLANT CELL | |
|---|---|---|---|