Subtilisin removes the surface layer of the phage fd coat.
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.
Schwind
P
P
Fakultät für Biologie, Universität Konstanz, Federal Republic of Germany.
Kramer
H
H
Kremser
A
A
Ramsberger
U
U
Rasched
I
I
D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000378:metabolism* / Q000648:ultrastructure; D002213:Capsid / Q000737:chemistry / Q000378:metabolism*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004563:Electrochemistry; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D013381:Subtilisins / Q000378:metabolism*
D010446:Peptide Fragments; D013381:Subtilisins