Asparaginase II of Saccharomyces cerevisiae. Characterization of the ASP3 gene

K. W. Kim, J. Q. Kamerud, D. M. Livingston, R. J. Roon

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Purified preparations of asparaginase II of Saccharomyces cerevisiae exhibit two protein bands upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Cloning and sequencing of the ASP3 gene, and partial amino acid sequencing as asparaginase II, imply that both bands are encoded by ASP3 but have different N termini. Northern blot analysis using the cloned ASP3 gene as a probe indicates that nitrogen catabolite repression of asparaginase II is achieved by alteration in mRNA levels. Deletion of sequences >600 base pairs upstream from the initiation AUG codon results in an altered response to certain nitrogen sources in strains containing the truncated gene.

Original languageEnglish (US)
Pages (from-to)11948-11953
Number of pages6
JournalJournal of Biological Chemistry
Issue number24
StatePublished - 1988


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