PMID:7968527
| Citation |
Mitchell, C and Oliver, D (1993) Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase. Mol. Microbiol. 10:483-97 |
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| Abstract |
Six putative ATP-binding motifs of SecA protein were altered by oligonucleotide-directed mutagenesis to try to define the ATP-binding regions of this multifunctional protein. The effects of the mutations were analysed by genetic and biochemical assays. The results show that SecA contains two essential ATP-binding domains. One domain is responsible for high-affinity ATP binding and contains motifs A0 and B0, located at amino acid residues 102-109 and 198-210, respectively. A second domain is responsible for low-affinity ATP binding and contains motifs A3 and a predicted B motif located at amino acid residues 503-511 and 631-653, respectively. The ATP-binding properties of both domains were essential for SecA-dependent translocation ATPase and in vitro protein translocation activities. The significance of these findings for the mechanism of SecA-dependent protein translocation is discussed. |
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| Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/physiology; Adenosine Triphosphate/metabolism; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacterial Proteins/physiology; Base Sequence; Binding Sites; Biological Transport, Active; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Membrane Transport Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Binding; Protein Structure, Tertiary; Sequence Alignment; Sequence Homology, Amino Acid; Subcellular Fractions/enzymology |
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