A novel family of carbohydrate-binding modules identified with Ruminococcus albus proteins

Xu, Qi, Morrison, Mark, Nelson, Karen E., Bayer, Edward, A., Atamna, Nof and Lamed, Raphael (2004) A novel family of carbohydrate-binding modules identified with Ruminococcus albus proteins. Febs Letters, 566 1-3: 11-16.


Author Xu, Qi
Morrison, Mark
Nelson, Karen E.
Bayer, Edward, A.
Atamna, Nof
Lamed, Raphael
Title A novel family of carbohydrate-binding modules identified with Ruminococcus albus proteins
Journal name Febs Letters  (ERA 2012 Listed)    (ERA 2010 Rank B)   Check publisher's open access policy
Publication date 2004-05
Sub-type Article
DOI 10.1016/j.febslet.2004.04.005
Volume number 566
Issue number 1-3
ISSN 0014-5793
Start page 11
End page 16
Total pages 6
Place of publication Amsterdam, Netherlands
Publisher Elseveir
Language eng
Subject 0601 Biochemistry and Cell Biology
0605 Microbiology
Abstract We recently showed that some of the enzymes underpinning cellulose solubilization by Ruminococcus albus 8 lack the conventional type of dockerin module characteristic of cellulosomal proteins and instead, bear an “X” domain of unknown function at their C-termini. We have now subcloned and expressed six X domains and showed that five of them bind to xylan, chitin, microcrystalline and phosphoric-acid swollen cellulose, as well as more heterogenous substrates such as alfalfa cell walls, banana stem and wheat straw. The X domain that did not bind to these substrates was derived from a family-5 glycoside hydrolase (Cel5G), which possesses two X domains in tandem. Whereas the internal X domain failed to bind to the substrates, the recombinant dyad exhibited markedly enhanced binding relative to that observed for the C-terminal X domain alone. The evidence supports a distinctive carbohydrate-binding role of broad specificity for this type of domain, and we propose a novel family (designated family 37) of carbohydrate-binding modules that appear to be peculiar to R. albus.
Keyword Ruminococcus albus
Carbohydrate binding molecules
Proteins
Q-Index Code C1

Document type: Journal Article
Sub-type: Article
Collections: Excellence in Research Australia (ERA) - Collection
School of Chemistry and Molecular Biosciences
 
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