PMID:10234835
| Citation |
Thomas, G, Potter, L and Cole, JA (1999) The periplasmic nitrate reductase from Escherichia coli: a heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site. FEMS Microbiol. Lett. 174:167-71 |
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| Abstract |
The periplasmic nitrate reductase, NapA, from Escherichia coli was identified as a 90 kDa molybdoprotein which comigrated during polyacrylamide gel electrophoresis with the di-haem c-type cytochrome, NapB. The DNA sequence of the 5' end of the napA gene and the N-terminal amino acid sequences of both NapA and NapB were determined. The 36 residue leader peptide for NapA includes the double-arginine motif typical of proteins to which complex redox cofactors are attached in the cytoplasm prior to targeting to the periplasm. The pre-NapA leader sequence is both unexpectedly long and, unless two successive proteolysis steps are involved, is cleaved at the unprecedented sequence G-Q-Q-. Nap activity was suppressed during growth in the presence of tungstate and was absent from a mutant unable to synthesise the molybdopterin cofactor. |
| Links | |
| Keywords |
Amino Acid Sequence; Arginine; Base Sequence; Coenzymes; Cytochrome c Group/isolation & purification; Dimerization; Escherichia coli/enzymology; Escherichia coli/genetics; Metalloproteins/metabolism; Molecular Sequence Data; Molybdenum; Nitrate Reductases/drug effects; Nitrate Reductases/genetics; Nitrate Reductases/isolation & purification; Periplasm/enzymology; Periplasm/genetics; Protein Precursors/genetics; Protein Sorting Signals/genetics; Pteridines/metabolism; Tungsten Compounds/pharmacology |
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