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.
journal_name
Proc Natl Acad Sci U S Aauthors
Perlman D,Raney P,Halvorson HOdoi
10.1073/pnas.83.14.5033subject
Has Abstractpub_date
1986-07-01 00:00:00pages
5033-7issue
14eissn
0027-8424issn
1091-6490journal_volume
83pub_type
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