AI Article Synopsis
- Aminopeptidase I is a key protein in the yeast Saccharomyces cerevisiae's transport pathway to the vacuole, known as the Cvt pathway, which is different from the classical protein transport routes.
- The protein forms a homododecameric complex in the cytoplasm, binds to the Atg19 receptor, and is transported to the vacuole packed in double-membrane vesicles.
- The chapter outlines methods for measuring the enzymatic activity of aminopeptidase I, which is essential for studying its assembly and transport, using techniques like spectrofluorometry and gel electrophoresis.
Article Abstract
Aminopeptidase I is the cargo protein of the cytoplasm-to-vacuole targeting (Cvt), autophagy-like protein-targeting pathway of the yeast Saccharomyces cerevisiae, the nonclassical vacuolar biosynthetic transport route. The second enzyme following this route to the vacuole, alpha-mannosidase, is also transported by direct binding to the Atg19 receptor and to aminopeptidase I. Aminopeptidase I forms a homododecameric complex, which is synthesized and assembled in the cytoplasm, packed in double-membrane vesicles, and transported to the vacuole. Only the homododecameric complex of aminopeptidase I has exopeptidase activity directed against amino-terminal leucine residues. Enzymatic activity can be determined spectrofluorometrically in homogenates and semi-quantitatively after nondenaturing gel electrophoresis and by yeast colony-overlay assay. This chapter describes the methods to determine aminopeptidase I enzymatic activity used to follow complex assembly and vacuolar transport.
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| http://dx.doi.org/10.1016/S0076-6879(08)03206-0 | DOI Listing |
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