Studies on the domain structure of the Salmonella typhimurium AraC protein.
The Salmonella typhimurium araC gene product is known to be susceptible to proteolytic degradation. Limited cleavage by trypsin, kallikrein, elastase and pronase E yields stable fragments comprising approximately the N-terminal two thirds of the AraC protein. These fragments have in common the ability to dimerize in solution and to bind L-arabinose and D-fucose. Under appropriate conditions, hydrolysis of the AraC protein with Staphylococcus aureus V8 protease leads to a small C-terminal fragment which is able to bind specifically to a synthetic ara consensus sequence. These results indicate that, as with several other prokaryotic gene regulatory proteins, the basic functions of effector binding, subunit interaction and specific DNA binding are segregated into distinct domains of the AraC protein.
Lauble
H
H
Abteilung Saenger, Institut für Kristallographie der Freien Universität Berlin.
Georgalis
Y
Y
Heinemann
U
U
D000595:Amino Acid Sequence; D051777:AraC Transcription Factor; D001089:Arabinose / Q000378:metabolism; D001426:Bacterial Proteins; D001483:Base Sequence; D003432:Cross-Linking Reagents; D004247:DNA / Q000138:chemical synthesis / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism; D005643:Fucose / Q000378:metabolism; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D010447:Peptide Hydrolases; D011487:Protein Conformation; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism; D012486:Salmonella typhimurium / Q000235:genetics / Q000378:metabolism*; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism
D051777:AraC Transcription Factor; D001426:Bacterial Proteins; D003432:Cross-Linking Reagents; D004268:DNA-Binding Proteins; D010446:Peptide Fragments; D012097:Repressor Proteins; D014157:Transcription Factors; D005643:Fucose; D004247:DNA; D001089:Arabinose; D010447:Peptide Hydrolases