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Relationship between utilization of dual translational initiation signals and protein processing in Streptomyces
Authors:Seiichi Taguchi  Ken-ichi Nishiyama  Izumi Kumagai  Haruo Momose and Kin-ichiro Miura
Institution:(1) Department of Biological Science and Technology, Science University of Tokyo, 278 Noda, Chiba, Japan;(2) Department of Industrial Chemistry, Faculty of Engineering, The University of Tokyo, 113 Bunkyo-ku, Tokyo, Japan
Abstract:Summary 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.Abbreviations SD Shine-Dalgarno - SSI Streptomyces subtilisin inhibitor
Keywords:Streptomyces subtilisin inhibitor (SSI) gene  Translation initiation  Initiation codon  Dual initiation sites for a protein gene  Protein processing
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