Asparaginase II of Saccharomyces cerevisiae. Characterization of the ASP3 gene.

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 greater than 600 base pairs upstream from the initiation AUG codon results in an altered response to certain nitrogen sources in strains containing the truncated gene.

• Publication year

  1988

• Venue

  Journal of Biological Chemistry

• Publication date

  1988-08-25

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/s0021-9258(18)37878-5PMID 3042786
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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