PMID:11513747
| Citation |
Ishii, Y and Amano, F (2001) Regulation of SulA cleavage by Lon protease by the C-terminal amino acid of SulA, histidine. Biochem. J. 358:473-80 |
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| Abstract |
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 accumulation and stability of the resulting mutant SulA proteins in vivo. Substitution of the extreme C-terminal histidine residue with another amino acid led to marked accumulation and high stability of SulA in lon(+) cells. A SulA mutant in which the C-terminal eight residues were deleted (SulAC161) showed high accumulation and stability, but the addition of histidine to the C-terminus of SulAC161 (SulAC161+H) made it labile. Similarly, SulAC161+H fused to maltose-binding protein (MBP-SulAC161+H) formed a tight complex with and was degraded rapidly by Lon in vitro. Histidine competitively inhibited the degradation of MBP-SulA by Lon, while other amino acids did not. These results suggest that the histidine residue at the extreme C-terminus of SulA is recognized specifically by Lon, leading to a high-affinity interaction between SulA and Lon. |
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| Keywords |
ATP-Binding Cassette Transporters; ATP-Dependent Proteases; Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Amino Acid Substitution; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Carrier Proteins/genetics; Escherichia coli Proteins; Heat-Shock Proteins/metabolism; Histidine/physiology; Maltose-Binding Proteins; Monosaccharide Transport Proteins; Mutation; Protease La; Recombinant Fusion Proteins/metabolism; Serine Endopeptidases/metabolism |
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