Molecular organisation of the malate synthase genes of Aspergillus nidulans and Neurospora crassa

✍ Scribed by Sandeman, Ruth A. ;Hynes, Michael J. ;Fincham, John R.S. ;Connerton, Ian F.

• Publisher: Springer
• Year: 1991
• Tongue: English
• Weight: 1000 KB
• Volume: 228
• Category: Article
• ISSN: 0026-8925
• DOI: 10.1007/bf00260638

✦ Synopsis

The sequencing and comparison of the genes encoding the glyoxylate bypass enzyme malate synthase of Aspergillus nidulans (acuE) and Neurospora crassa (acu-9) are presented. The predicted amino acid sequences of the A. nidulans and N. crassa enzymes are 538 and 542 residues respectively and the proteins are 87% homologous. In fungi, the malate synthase proteins are located in glyoxysomes and the deduced acuE and acu-9 proteins both contain a C-terminal S-K-L sequence, which has been implicated in transport into peroxisomes. The acuE coding region is interrupted by four introns and the acu-9 coding region is interrupted by one intron which occurs at the same position as the C-terminal acuE intron. The 5' non-coding regions of the two genes were examined for short homologous sequences that may represent the binding sites for regulatory proteins. Pyrimidine-rich sequences with weak homology to the amdI9 sequence, which has been implicated in facB-mediated acetate regulation of the amdS gene, were found but their functional significance remains to be determined.