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ARS Home » Research » Publications at this Location » Publication #97624
Title: GENE STRUCTURE OF A BIFUNCTIONAL CELLULASE GENE (CEL A) ISOLATED FROM TEREDINOBACTER TURNERAE

Author
item Freer, Shelby
item Skory, Christopher - Chris
item Bothast, Rodney
item Greene, Richard

Submitted to: American Chemical Society National Meeting
Publication Type: Abstract Only
Publication Acceptance Date: 3/25/1999
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Bacterial cultures (Teredinobacter turnerae) isolated from the gland of Deshayes of the marine shipworm (Psiloteredo healdi) produce extracellular cellulase activity when cultured with cellulose. The cel A gene of T. turnerae was isolated by screening a pUC 19 genomic DNA library for clearing of Ostrazin Brilliant Red-hydroxyethyl cellulose. Sequence analysis revealed that the cel A gene encodes a putative protein of 995 amino acids (104.5 kDa). There appears to be a multidomain structure consisting of a N-terminal endocellulase, two cellulose binding domains, and a C-terminal exocellulase. The four distinct regions are separated by three linker regions that are rich in serine and threonine. The endocellulase region is most closely related to cel E of P. fluorescens while the exocellulase region is most closely related to the cbh A gene of Cellulomonas fimi.