C-terminal identification of AD74, a proteolytic product of Enterococcus faecalis aggregation substance: application of liquid chromatography/mass spectrometry.
Sexual aggregation involved in conjugative transfer of Enterococcus faecalis plasmid pAD1 is enhanced by the sex pheromone cAD1, which is excreted from recipient cells. A membrane-anchored 137 kDa protein is a pAD1-encoded aggregation substance designated asal, which is responsible for cell-cell contact and leads to the aggregation of cells. An AD74 protein is a proteolytic product corresponding to the N-terminal half of asal. The C-terminal of AD74 was identified as lysine at position 510 (K-510) by liquid chromatography/mass spectrometry (LC/MS): it indicates that asal is cleaved specifically between K-510 and G-511.
Department of Agricultural Chemistry, University of Tokyo, Japan.
J
J
Nakayama
H
H
Watarai
A
A
Isogai
D B
DB
Clewell
A
A
Suzuki
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D015815:Cell Adhesion Molecules; D002449:Cell Aggregation; D002851:Chromatography, High Pressure Liquid; D013293:Enterococcus faecalis / Q000737:chemistry* / Q000235:genetics; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010449:Peptide Mapping; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D012697:Serine Endopeptidases
D001426:Bacterial Proteins; D015815:Cell Adhesion Molecules; D010446:Peptide Fragments; D011506:Proteins; C013065:cell aggregation factors; D012697:Serine Endopeptidases; C036813:lysyl endopeptidase