A single, phosphate-repressible deoxyribonuclease, DNase A, secreted in Aspergillus nidulans.

Abstract:

:High levels of nuclease activities were identified in filtrates of Aspergillus cultures after growth in low-but not in high-phosphate media. Deoxyribonuclease activities, characterized extensively by column chromatography, showed a coincident single peak for ss- and ds-DNase which was distinct from the peak for RNase. Both ss-DNase and ds-DNase are endonucleolytic and showed the highest activity in the presence of Ca2+ and Mn2+ (at pH 8.0). They also showed identical heat sensitivities suggesting that a single, phosphate-repressible DNase was secreted. This enzyme, therefore, corresponds to the well-characterized extracellular DNase A of Neurospora. However, the Aspergillus DNase A did not cross-react with antisera to secreted Neurospora nucleases and showed different chromatographic properties, and active peptides of different sizes were visualized on DNA activity gels. The increasing derepression of Aspergillus DNase A by decreasing phosphate levels was similar to that of secreted alkaline phosphatase and these increases were both abolished by the regulatory mutant palcA.

journal_name

Biochem Genet

journal_title

Biochemical genetics

authors

Käfer E,Tittler A,Fraser MJ

doi

10.1007/BF02401798

subject

Has Abstract

pub_date

1989-04-01 00:00:00

pages

153-66

issue

3-4

eissn

0006-2928

issn

1573-4927

journal_volume

27

pub_type

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