Different binding specificities of S-layer homology modules from Clostridium thermocellum AncA, Slp1, and Slp2
Date
2006-07Author
Zhao Guangshan.
Wamalwa Benson M.
Sakka M.
Kimura T.
Sakka K.
Type
ArticleLanguage
enMetadata
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S-layer homology (SLH) module polypeptides were derived from Clostridium thermocellum 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 C. thermocellum cell-wall preparations. rAncA-SLH associated with native peptidoglycan-containing sacculi from C. thermocellum, 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 Escherichia coli cells definitely confirmed that rSlp1-SLH and rSlp2-SLH specifically interacted with peptidoglycan but not with SCWP.
URI
http://www.unboundmedicine.com/medline/citation/16861798/Different_binding_specificities_of_S_layer_homology_modules_from_Clostridium_thermocellum_AncA_Slp1_and_Slp2_http://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/37836
http://www.ncbi.nlm.nih.gov/pubmed/16861798
Citation
Bioscience, biotechnology and biochemistry 70:7 2006 Jul pg 1636-41Publisher
School of Biological Sciences, University of Nairobi
Description
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