Structure of the Aspergillus niger pelA gene and its expression in Aspergillus niger and Aspergillus nidulans
- 1 September 1991
- journal article
- research article
- Published by Springer Nature in Current Genetics
- Vol. 20 (4) , 293-299
- https://doi.org/10.1007/bf00318518
Abstract
Aspergillus niger pectin lyases are encoded by a multigene family. The complete nucleotide sequence of the pectin lyase PLA-encoding gene pelA has been determined. Comparison of the deduced amino acid sequence with the deduced amino acid sequence of the other characterized pectin lyase, PLD, shows that the proteins share 69% amino acid identity. When grown on media with pectin as the sole carbon source, A. niger transformants containing multiple copies of the pelA gene show raised mRNA levels and overexpression of the gene product PLA compared with the wild-type strain. PLA was purified and characterized. In A. nidulans transformants PLA is also produced in medium containing a high concentration of glucose and no pectin.Keywords
This publication has 19 references indexed in Scilit:
- Studies on transformation of Escherichia coli with plasmidsPublished by Elsevier ,2006
- Cloning and expression of a second Aspergillus niger pectin lyase gene (pelA): Indications of a pectin lyase gene family in A. nigerCurrent Genetics, 1990
- Isolation and structure of the pectin lyase D-encoding gene from Aspergillus nigerGene, 1990
- Regulation of the Aspergillus nidulans pectate lyase gene (pelA).Plant Cell, 1989
- Recombinant dna in Filamentous Fungi: Progress and ProspectsCritical Reviews in Biotechnology, 1987
- Development of a high-frequency transforming vector for Aspergillus nidulansGene, 1985
- Gewinnung von pektinolytischen Enzymen ausAspergillus niger in SubmerskulturJournal of Basic Microbiology, 1984
- 3′ Non-coding region sequences in eukaryotic messenger RNANature, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Über die Bildung von ungesättigten Abbauprodukten durch ein pektinabbauendes EnzymHelvetica Chimica Acta, 1960