The influence of DNA binding protein on the substrate affinities of DNA polymerase from Ustilago maydis: One polymerase implicated in ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1976-01

AUTHORS

Geoffrey T. Yarranton, Peter D. Moore, Adonis Spanos

ABSTRACT

The DNA polymerase of Ustilago maydis is stimulated by a DNA binding protein from the same organism. Analysis of this stimulation shows that there is an increase in affinity for both substrates of the reaction. The apparent Km for deoxynucleoside triphosphates is decreased 3 fold, and that for denatured DNA by 4 fold. In both cases the maximum velocity (Vmax) is increased 1.2 to 1.4 fold. It is suggested that the variability in the affinity of the enzyme for deoxynucleoside triphosphates mediated by the binding protein may provide the basis for the UV sensitivity of pyrimidine auxotrophs in this organism. More... »

PAGES

215-218

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00269596

DOI

http://dx.doi.org/10.1007/bf00269596

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1016858388

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/934054


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