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Title: INTERRUPTED CATALYTIC DOMAIN STRUCTURES IN XYLANASES FROM TWO DISTANTLY RELATED STRAINS OF PREVOTELLA RUMINICOLA

Author
item FLINT, HARRY - ABERDEEN, UK
item Whitehead, Terence
item MARTIN, JENNIFER - ABERDEEN, UK
item GASPARIC, ALES - UNIV LJUBLJANA, SLOVENIA

Submitted to: Biochimica et Biophysica Acta
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/14/1997
Publication Date: N/A
Citation: N/A

Interpretive Summary: The breakdown and digestion of the fiber portion of feed material by farm animals such as cattle and sheep is incomplete. This digestion requires several different proteins produced by bacteria that live in the rumen (stomach) of these animals. One approach to increasing digestion of feed material by farm animals and to lower feed costs is to genetically modify rumen bacteria to produce more of the proteins. This report details the protein sequence similarities between fiber-degrading proteins from different rumen bacteria. These results will allow scientists to compare and contrast the different proteins and potentially introduce the genes for these proteins into the rumen bacteria for increased production.

Technical Abstract: Two xylanases from the rumen anaerobic bacterium Prevotella ruminicola were found to possess highly unusual structures in which their family 10 catalytic domains are interrupted by unrelated sequences. XynC from P. ruminicola B14 carries a 160 amino acid insertion while a P. ruminicola D31d xylanase carries an unrelated 280 amino acid insertion, containing an imperfect 130 amino acid duplication. Both regions of family 10 homology were shown to be essential for activity of the D31d enzyme.