Further characterization of a ribonucleotide-polymerizing enzyme from Histoplasma capsulatum. II. Possible role in cellular metabolism

George Boguslawski, William S. Oetting, Dean A. Stetler

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

An enzyme, ribonucleotide polymerase, isolated from the yeast phase of a fungus, Histoplasma capsulatum has been found to stimulate the incorporation of dTMP in the reaction catalysed by DNA polymerase from H. capsulatum and E. coli. The stimulation is dependent on the amount of ribonucleotide polymerase added. The data indicate that protein-protein interaction is responsible for the increase in DNA synthesis. It is suggested that ribonucleotide polymerase may be involved in supplying short RNA primers for DNA polymerase.

Original languageEnglish (US)
Pages (from-to)684-689
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume78
Issue number2
DOIs
StatePublished - Sep 23 1977

Bibliographical note

Funding Information:
by grants from NSF

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