Different Binding Specificities of S-Layer Homology Modules from Clostridium thermocellum AncA, Slp1, and Slp2
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S-layer homology (SLH) module polypeptides were derived from <I>Clostridium thermocellum</I> S-layer proteins Slp1 and Slp2 and cellulosome anchoring protein AncA as rSlp1-SLH, rSlp2-SLH, and rAncA-SLH respectively. Their binding specificities were investigated using <I>C. thermocellum</I> cell-wall preparations. rAncA-SLH associated with native peptidoglycan-containing sacculi from <I>C. thermocellum</I>, including both peptidoglycan and secondary cell wall polymers (SCWP), but not to hydrofluoric acid-extracted peptidoglycan-containing sacculi (HF-EPCS) lacking SCWPs, suggesting that SCWPs are responsible for binding with SLH modules of AncA. On the other hand, rSlp1-SLH and rSlp2-SLH associated with HF-EPCS, suggesting that these polypeptides had an affinity for peptidoglycan. A binding assay using a peptidoglycan fraction prepared from <I>Escherichia coli</I> cells definitely confirmed that rSlp1-SLH and rSlp2-SLH specifically interacted with peptidoglycan but not with SCWP.
- Agricultural and Biological Chemistry
Agricultural and Biological Chemistry 70(7), 1636-1641, 2006-07-23
Japan Society for Bioscience, Biotechnology, and Agrochemistry