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J. Biol. Chem., Vol. 263, Issue 18, 8953-8957, 06, 1988
SK Bhatnagar and MJ Bessman
The mutator gene, mutT, has been cloned into an expression vector and
overproduced in Escherichia coli. The gene product has been purified to
over 90% homogeneity as judged by gel electrophoresis and amino acid
analysis. The amino acid composition of the protein and the sequence of the
20 amino acids of the N-terminal region agree well with the nucleotide
sequence of the gene reported by Akiyama et al. (Akiyama, M., Horiuchi, T.,
and Sekiguchi, M. (1987) Mol. Gen. Genet. 206, 9-16) and indicate that the
first of the potential initiation codons (position 164) of the open reading
frame in the PvuII fragment carrying the mutT gene is the site of
initiation of translation of the 15,000-Da polypeptide. A novel nucleoside
triphosphatase activity which has a preference for dGTP is associated with
the purified protein, and preliminary experiments are consistent with the
notion that the mutT gene product is the enzyme responsible for this
activity.
Studies on the mutator gene, mutT of Escherichia coli. Molecular cloning of the gene, purification of the gene product, and identification of a novel nucleoside triphosphatase
McCollum-Pratt Institute, Johns Hopkins University, Baltimore, Maryland 21218.
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