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Characterization of the rough endoplasmic reticulum ribosome-binding activity
J M Nunnari1, D L Zimmerman, S C Ogg
1Department of Biochemistry and Biophysics, University of California Medical School, San Francisco 94143-0448.
Nature
|August 15, 1991
Summary
Researchers investigated rough endoplasmic reticulum ribosome receptors. They found that the previously identified ERp180 protein does not bind ribosomes, contrary to prior proposals. Ribosome-binding activity is associated with a different, smaller protein.
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Biochemistry
Background:
- Mammalian cell rough endoplasmic reticulum (RER) membranes possess specific sites for ribosome binding.
- A 180 kDa negatively charged protein, ERp180, was previously proposed to be the RER ribosome receptor.
Purpose of the Study:
- To re-evaluate the identity of the rough endoplasmic reticulum ribosome receptor.
- To determine if ERp180 functions as the RER ribosome receptor.
Main Methods:
- Solubilization of ribosome-binding activity from RER membranes.
- Biochemical fractionation and characterization of solubilized proteins.
- Cofractionation analysis of ribosome-binding activity and ERp180.
Main Results:
- Ribosome-binding site activity was quantitatively solubilized from RER membranes.
- The solubilized ribosome-binding activity did not cofractionate with the ERp180 protein.
- Ribosome-binding activity was found to be associated with a smaller, positively charged protein.
Conclusions:
- ERp180 is not the primary rough endoplasmic reticulum ribosome receptor.
- The RER ribosome receptor is a distinct, smaller, positively charged protein.
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