Unique N-Terminal Interactions Connect F-BOX STRESS INDUCED (FBS) Proteins to a WD40 Repeat-like Protein Pathway in Arabidopsis
| Autor: | Anneke A. Fleming, Elena C. Fulton, Joshua M. Gendron, Emily V. Parlan, Bryan Thines, Lily E. O’Connor, Edgar Sepúlveda-García, Mario Rocha-Sosa, Amy Replogle |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
F-box protein
Subfamily Ecology biology Chemistry SCF complex Botany Plant Science stress response Protein degradation biology.organism_classification Article Cell biology WD40 repeat-like protein WD40 repeat Ubiquitin QK1-989 Arabidopsis biology.protein Ecology Evolution Behavior and Systematics Function (biology) |
| Zdroj: | Plants Volume 10 Issue 10 Plants, Vol 10, Iss 2228, p 2228 (2021) |
| ISSN: | 2223-7747 |
| DOI: | 10.3390/plants10102228 |
| Popis: | SCF-type E3 ubiquitin ligases provide specificity to numerous selective protein degradation events in plants, including those that enable survival under environmental stress. SCF complexes use F-box (FBX) proteins as interchangeable substrate adaptors to recruit protein targets for ubiquitylation. FBX proteins almost universally have structure with two domains: A conserved N-terminal F-box domain interacts with a SKP protein and connects the FBX protein to the core SCF complex, while a C-terminal domain interacts with the protein target and facilitates recruitment. The F-BOX STRESS INDUCED (FBS) subfamily of plant FBX proteins has an atypical structure, however, with a centrally located F-box domain and additional conserved regions at both the N- and C-termini. FBS proteins have been linked to environmental stress networks, but no ubiquitylation target(s) or biological function has been established for this subfamily. We have identified two WD40 repeat-like proteins in Arabidopsis that are highly conserved in plants and interact with FBS proteins, which we have named FBS INTERACTING PROTEINs (FBIPs). FBIPs interact exclusively with the N-terminus of FBS proteins, and this interaction occurs in the nucleus. FBS1 destabilizes FBIP1, consistent with FBIPs being ubiquitylation targets SCFFBS1 complexes. This work indicates that FBS proteins may function in stress-responsive nuclear events, and it identifies two WD40 repeat-like proteins as new tools with which to probe how an atypical SCF complex, SCFFBS, functions via FBX protein N-terminal interaction events. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|