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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Xu Q,Morrison M,Nelson KE,Bayer EA,Atamna N,Lamed Rdoi
10.1016/j.febslet.2004.04.005keywords:
subject
Has Abstractpub_date
2004-05-21 00:00:00pages
11-6issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579304004296journal_volume
566pub_type
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