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Papers In Press, published online ahead of print September 17, 2001
J. Biol. Chem, 10.1074/jbc.M107143200
Submitted on July 27, 2001
Revised on September 17, 2001
Accepted on September 17, 2001
Biological and Nutritional Sciences, University of Newcastle Upon Tyne, Newcastle Upon Tyne, Tyne and Wear NE1 7RU
Corresponding Author: H.J.Gilbert{at}Newcastle.ac.uk
The recycling of photosynthetically fixed carbon, by the action of microbial plant cell wall hydrolases, is a fundamental biological process that has considerable industrial potential. Enzyme systems that attack the plant cell wall contain non-catalytic carbohydrate binding modules (CBMs) that mediate attachment to this composite structure, and maximise the hydrolytic process. Anaerobic fungi are the most efficient plant cell wall degraders known and this activity is vested in a protein complex that binds to the plant cell wall. To investigate whether plant cell wall attachment is mediated by non-catalytic proteins, a cDNA library of the anaerobic fungus Piromyces equi was screened for sequences that encode non-catalytic proteins that are components of the cellulase/hemicellulase complex. A 1.6 kb cDNA was isolated encoding a protein of 479 amino acids with a Mr 52548 designated NCP1. The protein had a modular architecture comprising three copies of the non-catalytic dockerin module that targets anaerobic fungal proteins to the cellulase/hemicellulase complex. The two C-terminal modules of NCP1, CBM29-1 and CBM29-2, respectively, exhibit 33 % sequence identity with each other, but have no homologues in protein databases. A truncated form of NCP1 comprising CBM29-1 and CBM29-2 (CBM29-1-2), and each of the two individual copies of CBM29, bind to mannan, cellulose and glucomannan, displaying highest affinity for glucomannan. CBM29-1-2 exhibits 4-45-fold higher affinity than either CBM29-1 or CBM29-2 for the various ligands, indicating that the two modules act in synergy to bind to the different polysaccharides. This paper provides the first report of a CBM-containing protein from an anaerobic fungal cellulase/hemicellulase complex. The two CBMs constitute a novel CBM family designated CBM29, whose members exhibit wide ligand specificity. We propose that NCP1 plays a pivotal role in sequestering the fungal enzyme complex onto the plant cell wall.
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