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Modification of yeast ribosomal proteins. Phosphorylation
The Biochemical Journal
|October 1, 1978
Summary
Yeast ribosomal proteins S2, S10, L9, L30, L44, and L45 are phosphorylated in vivo, primarily on serine residues. This phosphorylation likely impacts ribosome function rather than assembly.
Area of Science:
- Molecular Biology
- Biochemistry
- Cell Biology
Background:
- Ribosome biogenesis is a complex process involving numerous protein and RNA components.
- Post-translational modifications, such as phosphorylation, can regulate protein function and localization.
- Understanding the roles of specific ribosomal proteins is crucial for deciphering ribosome function.
Purpose of the Study:
- To identify phosphorylated ribosomal proteins in yeast.
- To investigate the stage at which phosphorylation occurs during ribosome assembly.
- To determine the potential functional implications of ribosomal protein phosphorylation.
Main Methods:
- Two-dimensional polyacrylamide-gel electrophoresis (2D-PAGE) was employed.
- Yeast cells were metabolically labeled in vivo using 32PO43-.
- Phosphorylated proteins were identified by analyzing the electrophoretic patterns.
Main Results:
- Specific proteins of the 40S (S2, S10) and 60S (L9, L30, L44, L45) ribosomal subunits were found to be phosphorylated.
- The majority of phosphate groups were attached to serine residues.
- The stoichiometry of phosphorylation was low, with 0.01 to 0.79 phosphate groups per molecule.
Conclusions:
- Phosphorylation of yeast ribosomal proteins occurs in vivo.
- These modifications are likely involved in ribosome function, not assembly, as they associate late in the process.
- Further research is needed to elucidate the precise functional roles of these phosphorylated ribosomal proteins.