Conformational alterations in the proximal portion of the yeast invertase signal peptide do not block secretion.
Various amino acid insertions have been introduced into the proximal portion of the signal sequence of secreted yeast invertase. The altered invertase genes have been reintroduced into yeast and monitored for their ability to direct synthesis of secreted invertase in vivo. The insertions should alter the signal polypeptide local secondary structure as predicted by the Chou and Fasman rules (1978). Secretion of these altered invertase polypeptides is not blocked by the amino acid insertions.
D001692:Biological Transport; D005796:Genes; D006026:Glycoside Hydrolases / Q000378:metabolism*; D010455:Peptides / Q000502:physiology*; D011487:Protein Conformation; D011498:Protein Precursors / Q000378:metabolism*; D021382:Protein Sorting Signals; D012441:Saccharomyces cerevisiae / Q000235:genetics; D013329:Structure-Activity Relationship; D043324:beta-Fructofuranosidase
D010455:Peptides; D011498:Protein Precursors; D021382:Protein Sorting Signals; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase