作者: R Young , C Y Chang , D L Smith
DOI:
关键词: Holin 、 Bacteriophage 、 Cell biology 、 Lysin 、 Ribosomal binding site 、 Integral membrane protein 、 Chemistry 、 Lysis 、 Transmembrane protein 、 Membrane protein
摘要: Most bacteriophages terminate infection by creating lesions in the cytoplasmic membrane, which not only cause immediate cell death but also allow escape of a phage-encoded endolysin. Destruction peptidoglycan and lysis follows very rapidly, allowing efficient release progeny virions. These membrane are formed small integral protein called holin. Holins have highly charged carboxyl-termini that thought to two transmembrane alpha-helical domains. believed oligomerize form large holes inner membrane. The prototype holin is S from bacteriophage lambda. Scheduling lytic event determined part "structure directed initiation" or sdi translational control region. Inductions S, cloned under variety native nonnative promoters with control, resulted at about 1000 molecules per cell, thus do produce biochemically useful amounts protein. By utilizing plasmid-based system T7 RNA polymerase promoter tandem consensus ribosome binding site, Coomassie blue-detectable quantities were obtained upon induction, corresponding an approximately 100-fold increase over normal lethal level Characterization this expression presented discussed respect current model function.