Subtilisin removes the surface layer of the phage fd coat
- 1 December 1992
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 210 (2) , 431-436
- https://doi.org/10.1111/j.1432-1033.1992.tb17438.x
Abstract
The major coat protein of native filamentous phage fd is vulnerable to digestion by subtilisin, but not by any of a number of other proteolytic enzymes. Degradation by the non-specific protease subtilisin occurs at specific sites in the N-terminal portion of g8p. The N-terminal part of the protein is considered to be the outer layer of a two-layered coat. Thus, subtilisin treatment results in a monolayered phage particle. These particles possess the morphology and stability of native phage fd. Furthermore, subtilisin proteolysis proved to be an efficient instrument in detecting variations in the topology of the g8p of related filamentous phages.Keywords
This publication has 38 references indexed in Scilit:
- Dissection of functional domains in phage fd adsorption proteinJournal of Molecular Biology, 1990
- Conformation of the coat protein of filamentous bacteriophage Pf1 determined by neutron diffraction from magnetically oriented gels of specifically deuterated virionsJournal of Molecular Biology, 1988
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985
- Structure similarity, difference and variability in the filamentous viruses fd, If1, IKe, Pf1 and XfJournal of Molecular Biology, 1983
- Domain structure of bacteriophage fd adsorption proteinFEBS Letters, 1981
- Chemical modification and molecular orientation of the B protein in the filamentous bacterial virus Pf1Journal of Molecular Biology, 1980
- Hydrodynamic properties and structure of fd virusJournal of Molecular Biology, 1977
- Studies on bacteriophage fd DNAJournal of Molecular Biology, 1977
- Mass, length, composition and structure of the filamentous bacterial virus fdJournal of Molecular Biology, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970