Dataset Information

Ribosomal protein turnover under normal condition

ABSTRACT: The cytosolic ribosome is composed of a large number of distinct protein types and its overall function is responsible for the synthesis of most proteins in plants. Defining the role of each of its protein subunits is a major challenge which is hampered by a lack of consistency in current attribution of proteins to the cytosolic ribosome or to the broader translatome associated with functioning ribosomes. The turover rates of several ribosomal proteins, including both small and large subunit proteins were measured, which showed that shows that some ribosomal proteins turnover much more rapidly that the ribosome as a whole and could be important to understand ribosome function, critical sites in their function or in vivo repair processes.

INSTRUMENT(S): 6340 Ion Trap LC/MS

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

TISSUE(S): Cell Culture

SUBMITTER: Karzan Salih

LAB HEAD: Harvey Millar

PROVIDER: PXD012839 | Pride | 2020-08-17

REPOSITORIES: Pride

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Publications

The composition and turnover of the Arabidopsis thaliana 80S cytosolic ribosome.

Salih Karzan Jalal KJ Duncan Owen O Li Lei L Trösch Josua J Millar A Harvey AH

The Biochemical journal 20200801 16

Cytosolic 80S ribosomes contain proteins of the mature cytosolic ribosome (r-proteins) as well as proteins with roles in ribosome biogenesis, protein folding or modification. Here, we refined the core r-protein composition in Arabidopsis thaliana by determining the abundance of different proteins during enrichment of ribosomes from cell cultures using peptide mass spectrometry. The turnover rates of 26 40S subunit r-proteins and 29 60S subunit r-proteins were also determined, showing that half o ...[more]

PMID: 32744327

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Project description:Functions of Arabidopsis REI1-LIKE (REIL) proteins, two homologs of a yeast ribosome biogenesis protein (RBP) that takes part in the late cytoplasmic steps of 60S ribosomal subunit maturation, were characterized by systems analyses of the 10°C cold acclimating reil1-1 reil2-1 double mutant compared to Col-0 wildtype. The mutant lacked both REIL proteins, was strongly growth inhibited in the cold and complemented by constitutive expression of N-terminal FLUORESCENT PROTEIN (FP)-REIL1 and FP-REIL2 fusion proteins under control of the UBIQUITIN 10 promoter. Wildtype acclimation to 10°C causes relative accumulation of cytosolic ribosome subunits and rRNA. Expression of cytosolic ribosomal genes, known cytosolic RBPs, translation initiation- and elongation-factors was activated. Conserved function of Arabidopsis REIL proteins was indicated by delay of these processes in reil1-1 reil2-1, cytosolic localization of FP-REIL proteins and native REIL protein interactions with 60S containing ribosome fractions. Non-acclimated reil1-1 reil2-1 triggered plant specific metabolic and transcriptomic cold acclimation responses that included activation of the DREB/CBF-regulon with a preference for the cold acclimation factors, CBF1/DREB1B, CBF2/DREB1C, and CBF3/DREB1A. Cold-acclimating reil1-1 reil2-1 maintained cellular integrity and acquired freezing tolerance but did not activate FLOWERING LOCUS T expression in mature leaves. This block was independent of FLOWERING LOCUS C and AGAMOUS-LIKE 19 mediated vernalization. We conclude that Arabidopsis REIL proteins enhance accumulation of cytosolic ribosome subunits after cold shift and either directly or indirectly feedback on temperature perception by suppression of premature cold acclimation at optimized temperature and by triggering growth and the vegetative to generative phase transition in the cold. Transcriptomic profiling demonstrated a hidden acclimation phenotype of the morphologically inconspicuous reil1-1reil2-1 mutant under optimized temperature conditions. Premature triggering of cold acclimation, a severe growth defect at 10°C and compensation responses indicate that REIL function may extend beyond cytosolic ribosome biogenesis towards translation initiation.

			Action	DRS
	F1_T1R1.dat	Other
	F1_T1R1.raw	Raw
	F1_T1R2.dat	Other
	F1_T1R2.raw	Raw
	F1_T1R3.dat	Other