Proteolytic enzymes are synthesized as inactive precursors, or “zymogens,” to prevent
unwanted protein degradation, and to enable spatial and temporal regulation of proteolytic …

Revised Manuscript Received April 11, 1994® abstract: Until quite recently it has been
generally believed that the observed tertiary structure of a protein is controlled by …

DNA polymerase enzymes make an error only once per 10 4–10 5 initial nucleotide
insertions during DNA replication. Most currently held models of this high fidelity cite the …

VPS10 (Vacuolar Protein Sorting) encodes a large type I transmembrane protein (Vps10p),
involved in the sorting of the soluble vacuolar hydrolase carboxypeptidase Y (CPY) to the …

The yeast vacuole, which is equivalent to the lysosome of higher eukaryotes, is one of the
best characterized degradative organelles. This review describes the biosynthesis and …

The precise shape of a protein is a crucial factor in its function. How do proteins become
folded into the right conformation? Molecular chaperones and protein folding catalysts bind …

Many proteins, including proteases and growth factors, are synthesized as precursors in the
form of prepro‐proteins. Whereas the pre‐sequences usually act as signal peptides for …

Bacterial Rhs proteins containing toxic domains are often secreted by type VI secretion
systems (T6SSs) through unclear mechanisms. Here, we show that the T6SS Rhs-family …

Revised Manuscript Received October 8, 1992 abstract: A peptide (PCB1) corresponding to
the proregion of the rat cysteine protease cathepsin B was synthesized and its ability to …

In vivo, many proteases are synthesized as larger precursors. During the maturation
process, the catalytically active protease domain is released from the larger polypeptide or …