The evolutionarily conserved Arabidopsis thaliana F-box protein AtFBP7 is required for efficient translation during temperature stress.
In eukaryotes, E3 ubiquitin ligases (E3s) mediate the ubiquitylation of proteins that are destined for degradation by the ubiquitin-proteasome system. In SKP1/CDC53/F-box protein (SCF)-type E3 complexes, the interchangeable F-box protein confers specificity to the E3 ligase through direct physical interactions with the degradation substrate. The vast majority of the approximately 700 F-box proteins from the plant model organism Arabidopsis thaliana remain to be characterized. Here, we investigate the previously uncharacterized and evolutionarily conserved Arabidopsis F-box protein 7 (AtFBP7), which is encoded by a unique gene in Arabidopsis (At1g21760). Several apparent fbp7 loss-of-function alleles do not have an obvious phenotype. AtFBP7 is ubiquitously expressed and its expression is induced after cold and heat stress. When following up on a reported co-purification of the eukaryotic elongation factor-2 (eEF-2) with YLR097c, the apparent budding yeast orthologue of AtFBP7, we discovered a general defect in protein biosynthesis after cold and heat stress in fbp7 mutants. Thus, our findings suggest that AtFBP7 is required for protein synthesis during temperature stress.
Calderón-Villalobos
Luz Irina A
LI
Department of Developmental Genetics, Centre for Plant Molecular Biology, Tübingen University, Auf der Morgenstelle 5, 72076 Tübingen, Germany.
Nill
Carola
C
Marrocco
Katia
K
Kretsch
Thomas
T
Schwechheimer
Claus
C
D000220:Adaptation, Biological / Q000235:genetics; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics* / Q000378:metabolism; D017124:Conserved Sequence; D019143:Evolution, Molecular; D044783:F-Box Proteins / Q000235:genetics* / Q000378:metabolism / Q000502:physiology*; D008969:Molecular Sequence Data; D010802:Phylogeny; D014176:Protein Biosynthesis; D017386:Sequence Homology, Amino Acid; D013696:Temperature; D014018:Tissue Distribution
D044783:F-Box Proteins