Modifications of Streptomyces signal peptides and their effects on protein production and secretion.
As for other organisms, proteins to be secreted in Streptomyces are produced as preproteins consisting of the mature protein preceded by a N-terminal signal peptide which is cleaved off during membrane translocation. Although primary sequences are seldom conserved among signal peptides, they all have a typical tripartite structure: a basic amino-terminus, a central apolar core and a carboxy-terminal region containing the signal peptidase recognition site. In vitro mutagenesis studies have been carried out on various signal peptides to analyse the structure-function relationship of each of the three regions of Streptomyces signal peptides. In the current paper the present knowledge of Streptomyces leader sequences and the impact of introduced mutations on transcription, translation and secretion of homologous and heterologous proteins is reviewed.
Lammertyn
E
E
Laboratory of Bacteriology, Rega Instituut, Katholieke Universiteit Leuven, Belgium.
Anné
J
J
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000378:metabolism*; D008969:Molecular Sequence Data; D016296:Mutagenesis; D021382:Protein Sorting Signals / Q000378:metabolism*; D013302:Streptomyces / Q000235:genetics* / Q000378:metabolism*
D001426:Bacterial Proteins; D021382:Protein Sorting Signals