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Title: Deletion of a Peptidylprolyl Isomerase Gene Results in the Inability of Caldicellulosiruptor bescii To Grow on Crystalline Cellulose without Affecting Protein Glycosylation or Growth on Soluble Substrates

Abstract

Caldicellulosiruptor bescii secretes a large number of complementary multifunctional enzymes with unique activities for biomass deconstruction. The most abundant enzymes in the C. bescii secretome are found in a unique gene cluster containing a glycosyl transferase (GT39) and a putative peptidyl prolyl cis-trans isomerase. Deletion of the glycosyl transferase in this cluster resulted in loss of detectable protein glycosylation in C. bescii, and its activity has been shown to be responsible for the glycosylation of the proline-threonine rich linkers found in many of the multifunctional cellulases. The presence of a putative peptidyl prolyl cis-trans isomerase within this gene cluster suggested that it might also play a role in cellulase modification. Here, we identify this gene as a putative prsA prolyl cis-trans isomerase. Deletion of prsA2 leads to the inability of C. bescii to grow on insoluble substrates such as Avicel, the model cellulose substrate, while exhibiting no differences in phenotype with the wild-type strain on soluble substrates. Finally, we provide evidence that the prsA2 gene is likely needed to increase solubility of multifunctional cellulases and that this unique gene cluster was likely acquired by members of the Caldicellulosiruptor genus with a group of genes to optimize the production and activitymore » of multifunctional cellulases.« less

Authors:
 [1];  [1];  [2];  [3];  [3];  [2]; ORCiD logo [3]; ORCiD logo [1]
  1. Univ. of Georgia, Athens, GA (United States); US Department of Energy (USDOE), Washington DC (United States)
  2. Univ. of Georgia, Athens, GA (United States)
  3. National Renewable Energy Lab. (NREL), Golden, CO (United States); US Department of Energy (USDOE), Washington DC (United States)
Publication Date:
Research Org.:
National Renewable Energy Lab. (NREL), Golden, CO (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER)
OSTI Identifier:
1660227
Report Number(s):
NREL/JA-2700-77675
Journal ID: ISSN 0099-2240; MainId:30590;UUID:8f436b9c-b145-47ba-892a-f147a0557a55;MainAdminID:17313
Grant/Contract Number:  
AC36-08GO28308
Resource Type:
Accepted Manuscript
Journal Name:
Applied and Environmental Microbiology
Additional Journal Information:
Journal Volume: 86; Journal Issue: 20; Journal ID: ISSN 0099-2240
Publisher:
American Society for Microbiology
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Caldicellulosiruptor bescii; enzymes; biomass

Citation Formats

Russell, Jordan F., Russo, Matthew L., Wang, Xuewen, Hengge, Neal, Chung, Daehwan, Wells, Lance, Bomble, Yannick, and Westpheling, Janet. Deletion of a Peptidylprolyl Isomerase Gene Results in the Inability of Caldicellulosiruptor bescii To Grow on Crystalline Cellulose without Affecting Protein Glycosylation or Growth on Soluble Substrates. United States: N. p., 2020. Web. https://doi.org/10.1128/aem.00909-20.
Russell, Jordan F., Russo, Matthew L., Wang, Xuewen, Hengge, Neal, Chung, Daehwan, Wells, Lance, Bomble, Yannick, & Westpheling, Janet. Deletion of a Peptidylprolyl Isomerase Gene Results in the Inability of Caldicellulosiruptor bescii To Grow on Crystalline Cellulose without Affecting Protein Glycosylation or Growth on Soluble Substrates. United States. https://doi.org/10.1128/aem.00909-20
Russell, Jordan F., Russo, Matthew L., Wang, Xuewen, Hengge, Neal, Chung, Daehwan, Wells, Lance, Bomble, Yannick, and Westpheling, Janet. Thu . "Deletion of a Peptidylprolyl Isomerase Gene Results in the Inability of Caldicellulosiruptor bescii To Grow on Crystalline Cellulose without Affecting Protein Glycosylation or Growth on Soluble Substrates". United States. https://doi.org/10.1128/aem.00909-20.
@article{osti_1660227,
title = {Deletion of a Peptidylprolyl Isomerase Gene Results in the Inability of Caldicellulosiruptor bescii To Grow on Crystalline Cellulose without Affecting Protein Glycosylation or Growth on Soluble Substrates},
author = {Russell, Jordan F. and Russo, Matthew L. and Wang, Xuewen and Hengge, Neal and Chung, Daehwan and Wells, Lance and Bomble, Yannick and Westpheling, Janet},
abstractNote = {Caldicellulosiruptor bescii secretes a large number of complementary multifunctional enzymes with unique activities for biomass deconstruction. The most abundant enzymes in the C. bescii secretome are found in a unique gene cluster containing a glycosyl transferase (GT39) and a putative peptidyl prolyl cis-trans isomerase. Deletion of the glycosyl transferase in this cluster resulted in loss of detectable protein glycosylation in C. bescii, and its activity has been shown to be responsible for the glycosylation of the proline-threonine rich linkers found in many of the multifunctional cellulases. The presence of a putative peptidyl prolyl cis-trans isomerase within this gene cluster suggested that it might also play a role in cellulase modification. Here, we identify this gene as a putative prsA prolyl cis-trans isomerase. Deletion of prsA2 leads to the inability of C. bescii to grow on insoluble substrates such as Avicel, the model cellulose substrate, while exhibiting no differences in phenotype with the wild-type strain on soluble substrates. Finally, we provide evidence that the prsA2 gene is likely needed to increase solubility of multifunctional cellulases and that this unique gene cluster was likely acquired by members of the Caldicellulosiruptor genus with a group of genes to optimize the production and activity of multifunctional cellulases.},
doi = {10.1128/aem.00909-20},
journal = {Applied and Environmental Microbiology},
number = 20,
volume = 86,
place = {United States},
year = {2020},
month = {10}
}

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