PMID:10556534
| Citation |
Makino, S, Makino, T, Abe, K, Hashimoto, J, Tatsuta, T, Kitagawa, M, Mori, H, Ogura, T, Fujii, T, Fushinobu, S, Wakagi, T, Matsuzawa, H and Makinoa, T (1999) Second transmembrane segment of FtsH plays a role in its proteolytic activity and homo-oligomerization. FEBS Lett. 460:554-8 |
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| Abstract |
The FtsH (HflB) protein of Escherichia coli is a membrane-bound ATP-dependent zinc protease. The role(s) of the N-terminal membrane-anchoring region of FtsH were studied by fusion with a maltose-binding protein (MBP) at five different N-termini of FtsH. The MBP-FtsH fusions were expressed in the cytoplasm of E. coli, and were purified as soluble proteins. The four longer constructs, which have a second transmembrane segment and the C-terminal cytoplasmic region in common, retained ATP-dependent protease activity toward heat-shock transcription factor sigma(32), and were found to be homo-oligomers. In contrast, the shortest construct which has the C-terminal cytoplasmic region but not the second transmembrane segment showed neither protease activity nor oligomerization. Therefore, the second transmembrane segment, which neighbors the C-terminal cytoplasmic region of the FtsH, participates in not only its membrane-anchoring, but also its protease activity and homo-oligomerization. |
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| Keywords |
ATP-Binding Cassette Transporters; ATP-Dependent Proteases; Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/metabolism; Amino Acid Motifs/genetics; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacterial Proteins/physiology; Carrier Proteins/chemistry; Carrier Proteins/genetics; Carrier Proteins/isolation & purification; Carrier Proteins/physiology; Cloning, Molecular; Escherichia coli Proteins; Histidine/genetics; Hydrolysis; Maltose-Binding Proteins; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Membrane Proteins/physiology; Monosaccharide Transport Proteins; Peptide Fragments/chemistry; Peptide Fragments/genetics; Peptide Fragments/metabolism; Peptide Fragments/physiology; Peptide Hydrolases/metabolism; Protein Structure, Secondary; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/isolation & purification; Ultracentrifugation |
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