Many random sequences functionally replace the secretion signal sequence of yeast invertase.
In the process of protein secretion, amino-terminal signal sequences are key recognition elements; however, the relation between the primary sequence of an amino-terminal peptide and its ability to function as an export signal remains obscure. The limits of variation permitted for functional signal sequences were determined by replacement of the normal signal sequence of Saccharomyces cerevisiae invertase with essentially random peptide sequences. Since about one-fifth of these sequences can function as an export signal the specificity with which signal sequences are recognized must be very low.
D000595:Amino Acid Sequence; D003593:Cytoplasm / Q000201:enzymology; D005110:Extracellular Space / Q000201:enzymology; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006031:Glycosylation; D021382:Protein Sorting Signals / Q000502:physiology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000378:metabolism; D013329:Structure-Activity Relationship; D043324:beta-Fructofuranosidase
D021382:Protein Sorting Signals; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase