Studies of the Path of Assembly of Bacteriophage M13 Coat Protein Into the Escherichia coli Cytoplasmic Membrane

作者: P. Hearne , M. Nokelainen , A. Ponticelli , Y. Hirota , K. Ito

DOI: 10.1007/978-3-642-81557-7_18

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摘要: Viruses have aided in the study of many biological processes such as DNA synthesis and transcriptional regulation. The capsid protein coliphage M13 offers several distinct advantages for membrane biogenesis: 1. It spans host cell plasma at each stage virus infection with its N-terminus on outer (periplasmic) surface (Wickner 1975, 1976) C-terminus exposed to cytoplasm (Webster Cashman 1978). 2. Its amino acid sequence that precursor form been independently determined by methods (von Wezenbeek et al. pers. commun.), RNA (Sugimoto 1977), sequencing (Asbeck 1969; Nakashima Konigsberg 1974). It entirely lacks four acids. 3. It is made great abundance infected cell, can account up 1/3 (Smilowitz 1972). 4. Its unusually small size allows it be directly assayed SDS polyacrylamide gel electrophoresis unfractionated, cells after pulse labeling radioactive acids (Ito 1980). 5. It readily isolated gram quantities (Knippers Hoffmann-Berling 1966; Woolford Webster 1975). 6. Antibodies prepared which are quite specific N-terminal 8 residues coat will cross-react procoat well 1980). 7. An amber mutant available gene other 7 genes (Henry Pratt 1969).

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