Article
Regulation of SulA cleavage by Lon protease by the C-terminal amino acid of SulA, histidine.
The Biochemical journal - 1 Sept 2001
Ishii Y, Amano F
Abstract excerpt
SulA protein, a cell division inhibitor in Escherichia coli, is degraded by Lon protease. The C-terminal eight residues of SulA have been shown to be recognized by Lon; however, it remains to be elucidated which amino acid in the C-terminus of SulA is critical for the recognition of SulA by Lon. To clarify this point, we constructed mutants of SulA with changes in the C-terminal residues, and examined the...
Topics
- ATP-Binding Cassette Transporters
- ATP-Dependent Proteases
- Adenosine Triphosphatases
- Amino Acid Sequence
- Amino Acid Substitution
- Bacterial Proteins
- Carrier Proteins
- Escherichia coli Proteins
- Heat-Shock Proteins
- Histidine
- Maltose-Binding Proteins
- Monosaccharide Transport Proteins
- Mutation
- Protease La
- Recombinant Fusion Proteins
- Serine Endopeptidases