J. Biol. Chem., Vol. 255, Issue 3, 917-921, Feb, 1980
Phenylglyoxal as a template site-specific reagent for DNA and RNA polymerases. Selective inhibition of initiation
A Srivastava and MJ Modak
Phenylglyoxal, an arginine-specific reagent, strongly inhibits DNA
polymerases isolated from eukaryotic, prokaryotic, and RNA tumor viral
sources as well as Escherichia coli RNA polymerase. The inhibitory action
of phenylglyoxal appears to be due to interference with the template
binding function of these enzymes and implies the presence of an arginine
residue at the template binding site of these enzymes from diverse sources
and suggests that template dependent DNA, and perhaps RNA polymerases, may
be mechanistically similar with respect to their template binding function.
In contrast, the activity of terminal deoxynucleotidyl-transferase, a
template-independent DNA polymerase isolated from calf thymus, is not
inhibited by phenylglyoxal. A detailed analysis of the inhibitory process
carried out using avian myeloblastosis virus (AMV) DNA polymerase as a test
enzyme revealed that inclusion of template-primer during the preincubation
with phenylglyoxal, but not substrate triphosphates or primer alone,
protects the enzyme against phenylglyoxal inactivation. Furthermore,
phenylglyoxal does not appear to inhibit the elongation of initiated DNA
strands, but blocks the reinitiation of DNA synthesis.
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