Isolation of a fourth cysteinyl-containing peptide of the alpha-subunit of the F1 ATPase from Escherichia coli necessitates revision of the DNA sequence.
The rapid determination of cysteinyl residues by Creighton's method [(1980) Nature 284, 487-489] led to the discovery of a discrepancy between protein and DNA sequence data in the alpha-subunit of the F1 ATPase from Escherichia coli [(1984) Arch. Biochem. Biophys. 229, 320-328]. We have isolated a cysteinyl-containing decapeptide from the alpha-subunit with a protein sequence (AGCAMGEYFR) which is only partially recognizable from DNA data. Re-sequencing of DNA in the region coding for the peptide has resulted in two corrections: insertion of a cytosine before position 715 and deletion of a thymine at position 731 of the uncA gene.
Stan-Lotter
H
H
Clarke
D M
DM
Bragg
P D
PD
D000595:Amino Acid Sequence; D001483:Base Sequence; D003545:Cysteine / Q000032:analysis*; D004269:DNA, Bacterial; D004274:DNA, Recombinant / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D007525:Isoelectric Focusing; D010446:Peptide Fragments / Q000032:analysis; D006180:Proton-Translocating ATPases / Q000032:analysis / Q000096:biosynthesis / Q000235:genetics*; D014357:Trypsin
D004269:DNA, Bacterial; D004274:DNA, Recombinant; D010446:Peptide Fragments; D014357:Trypsin; D006180:Proton-Translocating ATPases; D003545:Cysteine