Arabidopsis Immunoprecipitated Plastid Expressed YFP Proteomics Probing Gatcab-Dependent Mistranslation

ABSTRACT: Protein translation is a fundamental principle in cell biology. It requires transfer RNAs (tRNAs) loaded with their cognate amino acid to ensure the accurate incorporation of amino acid into the nascent peptide chain. Bacteria, mitochondria, and plastids synthesize glutaminyl -tRNAs (Gln-tRNAGln) for protein synthesis via an indirect pathway. tRNAGln is initially charged with glutamate by a non-discriminating aminoacyl-tRNA synthetase. Subsequently, tRNA-attached glutamine is produced by transamidation of the Glu-tRNAGln via the aminoacyl-tRNA amido-transferase complex GatCAB. Impaired function of amido-transferases has mostly negative effects in humans, yeast and bacteria. Interestingly however, in bacteria protein mistranslation through changed amido-transferase activity was shown as specialized strategy to survive adverse conditions, such as reactive oxygen stress, UV-light or inhibitor treatments. The consequences of decreased amido-transferase activity in plant and especially its plastids are unknown. Tampering with the plant amido-transferase should result in amino acid misincorporation for proteins synthesized in plastids and mitochondria while nuclear encoded proteins should not exhibit increased rate of Gln to Glu substitutions. Using this dataset, we aim to investigate this hypothesis on plastid expressed YFP which was immunoprecipitated from WT or gatb-1 plants.

INSTRUMENT(S):

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Leaf, Rosette

SUBMITTER: Benjamin Brandt  

LAB HEAD: Hans-Henning Kunz

PROVIDER: PXD057466 | Pride | 2026-06-08

REPOSITORIES: pride