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Appl. Environ. Microbiol., Apr 1996, 1329-1335, Vol 62, No. 4
Copyright © 1996, American Society for Microbiology

Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium

B Li, SR Nagalla and V Renganathan
Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science & Technology, Portland 97291-1000, USA.

Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme produced by cellulose-degrading cultures of the wood-degrading basidiomycete Phanerochaete chrysosporium. CDH contains one flavin adenine dinucleotide (FAD) and one heme b per molecule, and it oxidizes cellobiose to cellobionolactone. In this report, a 2.4-kb cDNA encoding CDH was isolated by screening an expression library of P. chrysosporium OGC101 with a CDH-specific polyclonal antibody. The cDNA encodes a 755- amino-acid protein with a predicted mass of 80,115 Da. Sequence analysis suggests that the heme domain is located at the N terminus and that the falvin domain is located at the C terminus. The flavin domain shows a beta 1-alpha A-beta 2 motif for FAD binding and has high sequence similarity to several FAD-dependent enzymes. Little sequence similarity to hemoflavoenzymes is found. CDH binds to cellulose similarly to cellulases. However, little sequence similarity is observed with the conserved cellulose-binding sequences of cellulases. This suggests that CDH might possess a specific sequence for cellulose binding which is different from that of cellulases. Northern (RNA) blot analysis of total RNA from cellulose-, glucose-, and cellobiose-grown P. chrysosporium indicated that CDH mRNA is produced only in cellulose- grown cells. This suggests that CDH expression is regulated at the transcriptional level by either cellulose or one of its degradation products. Southern blot analysis suggests the presence of only a single gene for CDH in P. chrysosporium OGC101.

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