E. Lammertyn et J. Anne, MODIFICATIONS OF STREPTOMYCES SIGNAL PEPTIDES AND THEIR EFFECTS ON PROTEIN-PRODUCTION AND SECRETION, FEMS microbiology letters, 160(1), 1998, pp. 1-10
As for other organisms, proteins to be secreted in Streptomyces are pr
oduced as preproteins consisting of the mature protein preceded by a N
-terminal signal peptide which is cleaved off during membrane transloc
ation. Although primary sequences are seldom conserved among signal pe
ptides, they all have a typical tripartite structure: a basic amino-te
rminus, a central apolar core and a carboxy-terminal region containing
the signal peptidase recognition site. In vitro mutagenesis studies h
ave been carried out on various signal peptides to analyse the structu
re-function relationship of each of the three regions of Streptomyces
signal peptides. In the current paper the present knowledge of Strepto
myces leader sequences and the impact of introduced mutations on trans
cription, translation and secretion of homologous and heterologous pro
teins is reviewed. (C) 1998 Federation of European Microbiological Soc
ieties. Published by Elsevier Science B.V.