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Human fibronectin is synthesized as a pre-propolypeptide
FEBS Letters
|October 20, 1986
Summary
Researchers identified a 26-amino acid signal peptide in human fibronectin (FN). This extracellular glycoprotein also undergoes N-terminal processing to remove a 5-amino acid pro-sequence.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Fibronectins (FNs) are extracellular glycoproteins composed of similar subunits.
- Subunit variations arise from alternative splicing of pre-mRNA.
- The complete amino acid sequence of human cellular FN has been recently elucidated.
Purpose of the Study:
- To determine the complete amino acid sequence of human cellular fibronectin.
- To identify the signal peptide and N-terminal processing of fibronectin.
Main Methods:
- cDNA cloning and sequencing of human cellular fibronectin.
- Deduction of amino acid sequences from cloned cDNA.
Main Results:
- Deduced a 26-amino acid signal peptide for fibronectin.
- Identified proteolytic processing at the N-terminus, removing a 5-amino acid pro-sequence (Ser-Lys-Ser-Lys-Arg).
- Characterized the pro-sequence as distinctive, hydrophilic, and basic.
Conclusions:
- The signal sequence of fibronectin conforms to the consensus format.
- Fibronectin undergoes specific N-terminal processing involving a unique pro-sequence.