Mutations affecting the signal sequence alter synthesis and secretion of yeast invertase.

Abstract:

:Insertion mutations previously constructed within the proximal region of the yeast invertase signal sequence did not interfere with secretion or glycosylation of the enzyme. We now describe deletion mutations within the same signal sequence. Large deletions truncating the hydrophobic core of the signal peptide prevented both secretion and glycosylation of the enzyme and increased the intracellular concentration of nonglycosylated invertase. This increase was coupled with the appearance of a new invertase polypeptide, 2 kilodaltons larger than cytoplasmic invertase. The new polypeptide was consistent in size with uncleaved (signal peptide intact) pre-secretory invertase previously identified by using in vitro translation (apparent molecular mass, 62 kilodaltons). The data on enzyme activity indicate that invertase whose secretion is aborted by large deletion mutations augments the normal pool of cytoplasmic invertase found in sucrose-fermenting yeast cells.

authors

Perlman D,Raney P,Halvorson HO

doi

10.1073/pnas.83.14.5033

subject

Has Abstract

pub_date

1986-07-01 00:00:00

pages

5033-7

issue

14

eissn

0027-8424

issn

1091-6490

journal_volume

83

pub_type

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