Mutational Analysis of the Vacuolar Sorting Signal of Procarboxypeptidase Y in Yeast Shows a Low Requirement for Sequence Conservation
Open Access
- 12 January 1996
- journal article
- Published by Elsevier
- Vol. 271 (2) , 841-846
- https://doi.org/10.1074/jbc.271.2.841
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- pH‐dependent processing of yeast procarboxypeptidase Y by proteinase A in vivo and in vitroEuropean Journal of Biochemistry, 1994
- The pro region required for folding of carboxypeptidase Y is a partially folded domain with little regular structural coreBiochemistry, 1993
- Short peptide domains target proteins to plant vacuolesCell, 1992
- Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant.The Journal of cell biology, 1991
- Yeast carboxypeptidase Y requires glycosylation for efficient intracellular transport, but not for vacuolar sorting, in vivo stability, or activityEuropean Journal of Biochemistry, 1991
- Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids.The Journal of cell biology, 1990
- Autoradiography using storage phosphor technologyElectrophoresis, 1990
- Identification of a peroxisomal targeting signal at the carboxy terminus of firefly luciferase.The Journal of cell biology, 1987
- Distinct sequence determinants direct intracellular sorting and modification of a yeast vacuolar proteaseCell, 1987
- Signal sequencesJournal of Molecular Biology, 1985