Peroxisome biogenesis in yeast.

Abstract:

:Eukaryotic cells have evolved a complex set of intracellular organelles, each of which possesses a specific complement of enzymes and performs unique metabolic functions. This compartmentalization of cellular functions provides a level of metabolic control not available to prokaryotes. However, it presents the eukaryotic cell with the problem of targeting proteins to their specific location(s). Proteins must be efficiently transported from their site of synthesis in the cytosol to their specific organelle(s). Such a process may require translocation across one or more hydrophobic membrane barriers and/or asymmetric integration into specific membranes. Proteins carry cis-acting amino acid sequences that serve to act as recognition motifs for protein sorting and for the cellular translocation machinery. Sequences that target proteins to the endoplasmic reticulum/secretory pathway, mitochondria, and chloroplasts are often present as cleavable amino-terminal extensions. In contrast, most peroxisomal proteins are synthesized at their mature size and are translocated to the organelle without any post-translational modification. This review will summarize what is known about how yeast solve the problem of specifically importing proteins into peroxisomes and will suggest future directions for investigations into peroxisome biogenesis in yeast.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Aitchison JD,Nuttley WM,Szilard RK,Brade AM,Glover JR,Rachubinski RA

doi

10.1111/j.1365-2958.1992.tb01780.x

subject

Has Abstract

pub_date

1992-12-01 00:00:00

pages

3455-60

issue

23

eissn

0950-382X

issn

1365-2958

journal_volume

6

pub_type

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