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Evidence for a major conformational change of coat protein in assembly of fl bacteriophage

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Abstract

RECENT structural studies1,2 indicate that the DNA of filamentous bacteriophages is enclosed in a sheath of α-helical coat protein. In the course of phage biosynthesis this protein is tightly bound to the membrane of the host (Escherichia coli)3,4. We present here the results of circular dichroism (CD) studies strongly suggesting that the protein has a quite different conformation in its membrane-bound state, so that a major conformational change must accompany incorporation into the virus.

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Authors and Affiliations

  1. Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, 27710

    YASUHIKO NOZAKI, BRIAN K. CHAMBERLAIN, ROBERT E. WEBSTER & CHARLES TANFORD

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  1. YASUHIKO NOZAKI
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  2. BRIAN K. CHAMBERLAIN
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  3. ROBERT E. WEBSTER
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  4. CHARLES TANFORD
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NOZAKI, Y., CHAMBERLAIN, B., WEBSTER, R. et al. Evidence for a major conformational change of coat protein in assembly of fl bacteriophage. Nature 259, 335–337 (1976). https://doi.org/10.1038/259335a0

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  • DOI: https://doi.org/10.1038/259335a0

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