Wang H, Jones R W
Purdue University, West Lafayette, IN 47907, USA.
Gene. 1995 May 26;158(1):125-8. doi: 10.1016/0378-1119(95)00094-m.
An endoglucanase-encoding clone (egl2) was isolated from the phytopathogenic soilborne deuteromycete fungus Macrophomina phaseolina (Mp). Clones were obtained from a cDNA library by functional expression in Escherichia coli. The egl2 clone hybridized to a 1.3-kb mRNA. Expression is induced by carboxymethylcellulose (CMC) and repressed by glucose. The deduced amino acid (aa) sequence revealed strong similarity to the egl3 from Trichoderma reesei (Tr) (72% for identical residues and 81% with conservative substitution over a span of 324 aa). The Mp egl2 lacks the cellulose-binding domain and linker region found in the Tr egl3. Different codon usage between the two fungi resulted in a much shorter span of nucleotide homology. The Egl2 protein cleaves cellodextrins with continguous beta, 1-4 linkages of four and larger, and shows activity against CMC and birchwood xylan.
