Author:

Keywords:

Bacterial Proteins, Glycoside Hydrolases, Membrane Proteins, Serine Endopeptidases, Streptomyces, Science & Technology, Life Sciences & Biomedicine, Microbiology, BACILLUS-SUBTILIS, FUNCTIONAL-ANALYSIS, GENOME SEQUENCE, EXPRESSION, IDENTIFICATION, CLONING, GENES, INHIBITOR, HOST, 06 Biological Sciences, 07 Agricultural and Veterinary Sciences, 11 Medical and Health Sciences, 30 Agricultural, veterinary and food sciences, 31 Biological sciences, 32 Biomedical and clinical sciences

Abstract:

Most bacteria contain one type I signal peptidase (SPase) for cleavage of signal peptides from secreted proteins. The developmental complex bacterium Streptomyces lividans has the ability to produce and secrete a significant amount of proteins and has four different type I signal peptidases genes (sipW, sipX, sipY, and sipZ) unusually clustered in its chromosome. Functional analysis of the four SPases was carried out by phenotypical and molecular characterization of the different individual sip mutants. None of the sip genes seemed to be essential for bacterial growth. Analysis of total extracellular proteins indicated that SipY is likely to be the major S. lividans SPase, since the sipY mutant strain is highly deficient in overall protein secretion and extracellular protease production, showing a delayed sporulation phenotype when cultured in solid medium.