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Identification of Changing Ribosome Protein Compositions using Mass Spectrometry.

Parimal Samir1,2, Christopher M Browne1, Rahul3

  • 1Department of Biochemistry, Vanderbilt University, Nashville, TN, 37235, USA.

Proteomics
|September 14, 2018
PubMed
Summary
This summary is machine-generated.

Ribosomes dynamically change protein composition. Yeast ribosomes with RPL8A or RPL8B proteins are not interchangeable, showing ribosomes adapt to environmental changes.

Keywords:
RPL8A/Bcarbon source switchribosome filterribosome heterogeneity

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Area of Science:

  • Molecular Biology
  • Proteomics
  • Yeast Genetics

Background:

  • Ribosomes, the protein synthesis machinery, are increasingly recognized for their regulatory roles in gene expression.
  • Emerging evidence suggests ribosomes are dynamic complexes that can alter their protein makeup based on environmental cues.

Purpose of the Study:

  • To investigate the dynamic nature of ribosomes by quantifying protein composition changes in Saccharomyces cerevisiae 80S ribosomes.
  • To determine if specific paralog ribosomal proteins impact ribosome function and adaptability to environmental stimuli.

Main Methods:

  • Quantitative mass spectrometry (MS) was employed to analyze protein composition changes in yeast ribosomes.
  • Yeast genetics and polysome profiling were utilized to assess the functional interchangeability of specific ribosomal proteins.

Main Results:

  • Significant shifts in the relative proportions of paralog yeast ribosomal proteins RPL8A (eL8A) and RPL8B (eL8B) were observed in 80S ribosomes when switching yeast growth from glucose to glycerol.
  • Functional assays demonstrated that yeast ribosomes containing either RPL8A or RPL8B are not functionally equivalent.

Conclusions:

  • The findings support the hypothesis that ribosomes are dynamic entities capable of altering their protein composition.
  • These compositional changes correlate with altered functional activity, enabling adaptation to different growth and environmental conditions.