caa a22 4500 397556195 CHVBK 20180308164802.0 cr unu---uuuuu 161202e199606 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021348 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021348 The Virion Proteins Encoded by Bacteriophage φK and Its Host-Range Mutant φKhT: Host-Range Determination and DNA Binding Properties [Elektronische Daten] [Ken-Ichi Kodaira, Masaya Oki, Makiko Kakikawa, Hisashi Kimoto, Akira Taketo] The microvirid phage φK, specific for Escherichia coli K12, contains a circular single-stranded (SS) DNA in the icosahedral virion, which comprises four phage gene products, F (capsid), G (major spike), H (minor spike), and J (core). φKhT, a host-range mutant of φK, can grow on E. coli C and B, besides K12, and is more thermosensitive than the parental phage φK. Sequencing analysis revealed that the genome of φK and φKhT consists of 6,089 nucleotides (nt), and codes for eleven genes, whose sequences are similar to those of α3, φX174, and G4 infective to strain C. In φKhT, two nt had changed: one is in the gene G, resulting in replacement of the 75th codon Ala with Ser, and the other is at 67th codon of the gene H: Val to Ala. Chemically synthesized gene J protein composed of 23 amino acids (aa) binds to φK SS DNA more tightly than and preferentially over the host E. coli SS-DNA-binding protein (SSB). These results indicate that the two spike proteins G and H are involved in the determination of φK host-range, and support a model in which the gene J protein functions in packaging the viral SS DNA into the virion vesicle. © by the Journal of Biochemistry Regular Papers nationallicence bacteriophage nationallicence DNA-binding protein nationallicence host-range nationallicence φK nationallicence virion proteins nationallicence Kodaira Ken-Ichi Molecular Biology Group, Chemical and Biochemical Engineering, Faculty of Engineering, Toyama University 3190 Gofuku, Toyama, Toyama 930 aut Oki Masaya Molecular Biology Group, Chemical and Biochemical Engineering, Faculty of Engineering, Toyama University 3190 Gofuku, Toyama, Toyama 930 aut Kakikawa Makiko Molecular Biology Group, Chemical and Biochemical Engineering, Faculty of Engineering, Toyama University 3190 Gofuku, Toyama, Toyama 930 aut Kimoto Hisashi Department of Biochemistry I, Fukui Medical School Matsuoka, Fukui 910-11 aut Taketo Akira Department of Biochemistry I, Fukui Medical School Matsuoka, Fukui 910-11 aut The Journal of Biochemistry Oxford University Press 119/6(1996-06), 1062-1069 0021-924X 119:6<1062 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021348 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021348 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kodaira Ken-Ichi Molecular Biology Group, Chemical and Biochemical Engineering, Faculty of Engineering, Toyama University 3190 Gofuku, Toyama, Toyama 930 aut NATIONALLICENCE 700 1- Oki Masaya Molecular Biology Group, Chemical and Biochemical Engineering, Faculty of Engineering, Toyama University 3190 Gofuku, Toyama, Toyama 930 aut NATIONALLICENCE 700 1- Kakikawa Makiko Molecular Biology Group, Chemical and Biochemical Engineering, Faculty of Engineering, Toyama University 3190 Gofuku, Toyama, Toyama 930 aut NATIONALLICENCE 700 1- Kimoto Hisashi Department of Biochemistry I, Fukui Medical School Matsuoka, Fukui 910-11 aut NATIONALLICENCE 700 1- Taketo Akira Department of Biochemistry I, Fukui Medical School Matsuoka, Fukui 910-11 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/6(1996-06), 1062-1069 0021-924X 119:6<1062 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford