Cloning and sequence of a thermostable multidomain xylanase from the bacterium Rhodothermus marinus.
The gene (xyn1) encoding a Rhodothermus marinus xylanase has been cloned and expressed in Escherichia coli. The gene comprises 5 different domains in an unusual combination. The cellulose binding domains (CBDs) encoded by xyn1 are repeated in tandem at the N-terminus and show similarity with the CBD family IV. The xyn1-gene is the first example encoding a CBD family IV in combination with a xylan hydrolyzing catalytic domain of the glycosyl hydrolase family 10.
Nordberg Karlsson
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Department of Biotechnology, Center for Chemistry and Chemical Engineering, Lund University, Sweden. eva.nordberg-karlsson@biotek.lu.se
Bartonek-Roxå
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Holst
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D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D043364:Endo-1,4-beta Xylanases; D005798:Genes, Bacterial; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D014995:Xylosidases / Q000235:genetics*
D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases