Hydrophilic domains of scaffolding protein CbpA promote glycosyl hydrolase activity and localization of cellulosomes to the cell surface of Clostridium cellulovorans

Journal of Bacteriology
Akihiko KosugiRoy H Doi

Abstract

CbpA, the scaffolding protein of Clostridium cellulovorans cellulosomes, possesses one family 3 cellulose binding domain, nine cohesin domains, and four hydrophilic domains (HLDs). Among the three types of domains, the function of the HLDs is still unknown. We proposed previously that the HLDs of CbpA play a role in attaching the cellulosome to the cell surface, since they showed some homology to the surface layer homology domains of EngE. Several recombinant proteins with HLDs (rHLDs) and recombinant EngE (rEngE) were examined to determine their binding to the C. cellulovorans cell wall fraction. Tandemly linked rHLDs showed higher affinity for the cell wall than individual rHLDs showed. EngE was shown to have a higher affinity for cell walls than rHLDs have. C. cellulovorans native cellulosomes were found to have higher affinity for cell walls than rHLDs have. When immunoblot analysis was carried out with the native cellulosome fraction bound to cell wall fragments, the presence of EngE was also confirmed, suggesting that the mechanism anchoring CbpA to the C. cellulovorans cell surface was mediated through EngE and that the HLDs play a secondary role in the attachment of the cellulosome to the cell surface. During a study of...Continue Reading

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Citations

Aug 19, 2007·Journal of Bacteriology·Satoshi MatsuokaRoy H Doi
Apr 9, 2010·Annual Review of Biochemistry·Carlos M G A Fontes, Harry J Gilbert
Dec 22, 2007·Annals of the New York Academy of Sciences·Roy H Doi
Jul 23, 2014·Asian-Australasian Journal of Animal Sciences·SooYeon LimJongsoo Chang
Jul 23, 2013·Applied and Environmental Microbiology·Sang Duck JeonSung Ok Han
Jul 26, 2019·Environmental Microbiology Reports·Pierre SivadonRégis Grimaud
Aug 28, 2020·Frontiers in Bioengineering and Biotechnology·Andika SidarPeter J Punt

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