Abstract

The eukaryotic ribosome is a large molecular machine consisting of ~80 ribosomal proteins and 4 rRNAs. The 40S and 60S ribosomal subunits are assembled in the nucleolus by ~200 helper proteins then shipped into the cytoplasm or to the endoplasmic reticulum where protein translation takes place. Eventually ribosomes are removed from the cytoplasm and recycled through ribophagy, however, very is little is known about ribosomal protein exchange after assembly but before ribophagy. Using kinetic turnover measurements of ribosomal proteins and rRNA in vivo we determined ribosomal protein replacement rates are diverse suggesting ribosomal components may be replaced without destruction of the entire ribosome. Measurements from ad libitum fed and dietary restricted mice provide strong evidence that RPL10 exchanges rates are dramatically different between AL and DR while synthesis and degradation do not change. RPL10 turnover can be described using a two-pool kinetic model, which may be applied to many ribosomal proteins.

Degree

MS

College and Department

Physical and Mathematical Sciences; Chemistry and Biochemistry

Rights

http://lib.byu.edu/about/copyright/

Date Submitted

2015-08-01

Document Type

Thesis

Handle

http://hdl.lib.byu.edu/1877/etd8092

Keywords

ribosome, ribophagy, turnover, kinetics, proteomics, mass spectrometry, dietary restriction

Included in

Chemistry Commons

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