Homologous expression of the Caldicellulosiruptor bescii CelA reveals that the extracellular protein is glycosylated

Chung, Daehwan; Young, Jenna; Bomble, Yannick J.; Vander Wall, Todd A.; Groom, Joseph; Himmel, Michael E.; Westpheling, Janet

doi:10.1371/journal.pone.0119508

Title: Homologous expression of the Caldicellulosiruptor bescii CelA reveals that the extracellular protein is glycosylated

Journal Article · 23 March 2015 · PLoS ONE

DOI: https://doi.org/10.1371/journal.pone.0119508 · OSTI ID:1220729

Chung, Daehwan ^[1]; Young, Jenna ^[1]; Bomble, Yannick J. ^[2]; Vander Wall, Todd A. ^[2]; Groom, Joseph ^[1]; Himmel, Michael E. ^[2]; Westpheling, Janet ^[1]

Univ. of Georgia, Athens, GA (United States). Dept. of Genetics; Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). The BioEnergy Science Center
National Renewable Energy Lab. (NREL), Golden, CO (United States). Biosciences Center; Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). The BioEnergy Science Center

Members of the bacterial genus Caldicellulosiruptor are the most thermophilic cellulolytic microbes described with ability to digest lignocellulosic biomass without conventional pretreatment. The cellulolytic ability of different species varies dramatically and correlates with the presence of the multimodular cellulase CelA, which contains both a glycoside hydrolase family 9 endoglucanase and a glycoside hydrolase family 48 exoglucanase known to be synergistic in their activity, connected by three cellulose-binding domains via linker peptides. This architecture exploits the cellulose surface ablation driven by its general cellulase processivity as well as excavates cavities into the surface of the substrate, revealing a novel paradigm for cellulase activity. We recently reported that a deletion of celA in C. bescii had a significant effect on its ability to utilize complex biomass. To analyze the structure and function of CelA and its role in biomass deconstruction, we constructed a new expression vector for C. bescii and were able, for the first time, to express significant quantities of full-length protein in vivo in the native host. The protein, which contains a Histidine tag, was active and excreted from the cell. Expression of CelA protein with and without its signal sequence allowed comparison of protein retained intracellularly to protein transported extracellularly. Analysis of protein in culture supernatants revealed that the extracellular CelA protein is glycosylated whereas the intracellular CelA is not, suggesting that either protein transport is required for this post-translational modification or that glycosylation is required for protein export. The mechanism and role of protein glycosylation in bacteria is poorly understood and the ability to express CelA in vivo in C. bescii will allow the study of the mechanism of protein glycosylation in this thermophile. Finally, it will also allow the study of glycosylation of CelA itself and its role in the structure and function of this important enzyme in biomass deconstruction.

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Research Organization:: National Renewable Energy Laboratory (NREL), Golden, CO (United States); Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: 10-21-RR093-367

OSTI ID:: 1220729

Report Number(s):: NREL/JA-2700-64060

Journal Information:: PLoS ONE, Vol. 10, Issue 3; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 36 works

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
glycosylation
signal peptides
vector construction
cellulases
glycoproteins
plasmid construction
protein expression
uracils