Targeting of aminopeptidase I to the yeast vacuole ts mediated by Ssa1p, acytosolic member of the 70-kDa stress protein family

Citation
E. Silles et al., Targeting of aminopeptidase I to the yeast vacuole ts mediated by Ssa1p, acytosolic member of the 70-kDa stress protein family, J BIOL CHEM, 275(44), 2000, pp. 34054-34059
Citations number
29
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN journal
00219258 → ACNP
Volume
275
Issue
44
Year of publication
2000
Pages
34054 - 34059
Database
ISI
SICI code
0021-9258(20001103)275:44<34054:TOAITT>2.0.ZU;2-2
Abstract
The two cytosolic members of the highly conserved 70-kDa stress protein fam ily, Ssa1p and Ssa2p, were specifically retained by the prepro-NH2 extensio n of the vacuolar aminopeptidase I precursor (pAPI) conjugated to agarose ( Sulfolink). A temperature-sensitive mutant strain a1(ts)a234 (ssa1(ts) ssa2 ssa3 ssa4), when incubated at the restrictive temperature, was able to ass emble the API precursor into dodecamers, but failed to pack pAPI into vesic les and to convert it into mature API (mAPI), a process that occurs in the vacuole. Altogether these results indicate that Ssa1p mediates the targetin g of pAPI to the vacuole.