Proteome of the large Pseudomonas myovirus 201 phi 2-1: delineation of proteolytically processed virion proteins.

ABSTRACT: Pseudomonas chlororaphis phage 201 phi 2-1 produces a large structurally complex virion, including the products of 89 phage genes. Many of these proteins are modified by proteolysis during virion maturation. To delineate the proteolytic maturation process, 46 slices from an SDS-polyacrylamide gel were subjected to tryptic digestion and then HPLC-electrospray ionization-tandem mass spectrometry analysis. The scale of the experiment allowed high sequence coverage and detection of mass spectra assigned to peptides with one end produced by trypsin and the other end derived from a maturation cleavage (semitryptic peptides). Nineteen cleavage sites were detected in this way. From these sites, a cleavage motif was defined and used to predict the remaining cleavages required to explain the gel mob

SUBMITTER: Thomas JA 

PROVIDER: S-EPMC2871425 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature