Plant Signaling: Ubiquitin Pulls the Trigger on Chloroplast Degradation
نویسندگان
چکیده
Diverse proteolytic pathways regulate chloroplasts. Recent work has revealed significant new roles for chloroplast ubiquitination in stress adaptation, involving targeted protein removal through the ubiquitin-proteasome system, or selective, whole-chloroplast degradation.
منابع مشابه
Focus on ubiquitin in plant biology.
Ubiquitin and ubiquitin-like modifiers are small proteins that are covalently joined via their C-terminal carboxyl group to substrate proteins, often on a Lys residue, thereby modifying the stability, localization, or function of the target. Although ubiquitin is present in all eukaryotes, plants have an inordinate fondness for ubiquitin, as judged by the plethora of ubiquitin-protein ligases e...
متن کاملBlocking the Metabolism of Starch Breakdown Products in Arabidopsis Leaves Triggers Chloroplast Degradation
In most plants, a large fraction of photo-assimilated carbon is stored in the chloroplasts during the day as starch and remobilized during the subsequent night to support metabolism. Mutations blocking either starch synthesis or starch breakdown in Arabidopsis thaliana reduce plant growth. Maltose is the major product of starch breakdown exported from the chloroplast at night. The maltose exces...
متن کاملRole of Ubiquitin-Mediated Degradation System in Plant Biology
Ubiquitin-mediated proteasomal degradation is an important mechanism to control protein load in the cells. Ubiquitin binds to a protein on lysine residue and usually promotes its degradation through 26S proteasome system. Abnormal proteins and regulators of many processes, are targeted for degradation by the ubiquitin-proteasome system. It allows cells to maintain the response to cellular level...
متن کاملUbiquitin–Proteasome-Dependent Regulation of Bidirectional Communication between Plastids and the Nucleus
Plastids are DNA-containing organelles and can have unique differentiation states depending on age, tissue, and environment. Plastid biogenesis is optimized by bidirectional communication between plastids and the nucleus. Import of nuclear-encoded proteins into plastids serves as anterograde signals and vice versa, plastids themselves send retrograde signals to the nucleus, thereby controlling ...
متن کاملThe chloroplast protease subunit ClpP4 is a substrate of the E3 ligase AtCHIP and plays an important role in chloroplast function.
Animal CHIP proteins are chaperone-dependent E3 ubiquitin ligases that physically interact with Hsp70, Hsp90 and proteasome, promoting degradation of a selective group of non-native or damaged proteins in animal cells. The plant CHIP-like protein, AtCHIP, also plays important roles in protein turnover metabolism. AtCHIP interacts with a proteolytic subunit, ClpP4, of the chloroplast Clp proteas...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Current Biology
دوره 26 شماره
صفحات -
تاریخ انتشار 2016