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Structure and biosynthesis of the signal-sequence receptor
1Institut für Biochemie, Humboldt-Universität, Berlin, German Democratic Republic.
European Journal of Biochemistry
|March 10, 1990
Summary
The signal-sequence receptor (SSR) glycoprotein
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Biochemistry
Background:
- The signal-sequence receptor (SSR) is a known component of the endoplasmic reticulum (ER) membrane.
- Nascent polypeptides interact with the SSR during translocation across the ER membrane.
Purpose of the Study:
- To elucidate the primary structure of the signal-sequence receptor (SSR).
- To understand the molecular mechanisms governing SSR insertion and function within the ER membrane.
Main Methods:
- Deduction of primary structure from cDNA clones.
- Direct protein sequencing.
- Analysis of protein charge distribution and phosphorylation.
- Immunofluorescence microscopy for ER localization confirmation.
Main Results:
- The SSR is a glycoprotein synthesized with a cleavable signal sequence.
- It possesses a single membrane-spanning segment and exhibits distinct charge distribution at its termini.
- SSR insertion into the ER membrane is dependent on the signal-recognition particle.
- The cytoplasmic tail of SSR is phosphorylatable, suggesting functional regulation.
Conclusions:
- The primary structure of SSR reveals key features for its ER membrane integration and function.
- Phosphorylation of the SSR cytoplasmic tail indicates a regulatory mechanism.
- SSR plays a critical role in protein translocation into the ER.