Relationship between utilization of dual translational initiation signals and protein processing in Streptomyces.
Two sets of the Shine-Dalgarno sequence and the initiation codon (ATG) for translation of a gene encoding the protein SSI (Streptomyces subtilisin inhibitor) were studied in vivo by site-directed mutagenesis. The result shows that each ATG can function as an initiator of translation in either Streptomyces lividans 66 or Escherichia coli. The choice of initiation codon seems dependent on the host strain and is closely related to the processing mechanism of pre-SSI protein. The upstream ATG is presumed to be utilized preferentially giving two cleavage sites in pre-SSI in S. albogriseolus S-3253, the original SSI producer strain.
Taguchi
S
S
Department of Biological Science and Technology, Science University of Tokyo, Chiba, Japan.
Nishiyama
K
K
Kumagai
I
I
Momose
H
H
Miura
K
K
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001483:Base Sequence; D003062:Codon; D004269:DNA, Bacterial; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010442:Peptide Chain Initiation, Translational; D014176:Protein Biosynthesis / Q000235:genetics*; D011499:Protein Processing, Post-Translational / Q000235:genetics*; D021382:Protein Sorting Signals; D013302:Streptomyces / Q000235:genetics; D014169:Transformation, Bacterial
D001426:Bacterial Proteins; D003062:Codon; D004269:DNA, Bacterial; D021382:Protein Sorting Signals; C018150:subtilisin inhibitor protein, Streptomyces