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Ovalbumin utilizes an NH2-terminal signal sequence.
The Journal of Biological Chemistry
|April 25, 1982
Summary
Ovalbumin glycosylation and segregation into microsomes depend on signal sequence proximity. Microsomes must be added before the ovalbumin polypeptide chain reaches 150 amino acids for proper processing.
Area of Science:
- Molecular Biology
- Cell Biology
- Protein Biochemistry
Background:
- Protein glycosylation and segregation are crucial post-translational modifications.
- The "signal" sequence directs proteins to specific cellular compartments, like the endoplasmic reticulum.
Purpose of the Study:
- To determine the critical timing for microsome addition during ovalbumin synthesis for glycosylation and segregation.
- To investigate the location of the ovalbumin "signal" sequence.
Main Methods:
- Synchronized translation experiments using wheat germ and reticulocyte lysate systems.
- Addition of dog pancreatic microsomes at different time points during ovalbumin synthesis.
Main Results:
- Ovalbumin glycosylation and segregation occurred only when microsomes were added before the nascent polypeptide chain had 150 amino acids.
- This finding suggests the "signal" sequence is located prior to residue 150.
Conclusions:
- The timing of microsome addition is critical for the proper processing of ovalbumin.
- The "signal" sequence of ovalbumin is likely located before amino acid residue 150, contradicting previous reports.