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Title: Glycoside hydrolase gene transcription by Alicyclobacillus acidocaldarius during growth on wheat arabinoxylan and monosaccharides: a proposed xylan hydrolysis mechanism

Metabolism of carbon bound in wheat arabinoxylan (WAX) polysaccharides by bacteria requires a number of glycoside hydrolases active toward different bonds between sugars and other molecules. Alicyclobacillus acidocaldarius is a Gram-positive thermoacidophilic bacterium capable of growth on a variety of mono-, di-, oligo-, and polysaccharides. Nineteen proposed glycoside hydrolases have been annotated in the A. acidocaldarius Type Strain ATCC27009/DSM 446 genome. Here, experiments were performed to understand the effect of monosaccharides on gene expression during growth on the polysaccharide, WAX.
Authors:
ORCiD logo [1] ;  [2] ;  [3] ;  [4]
  1. Idaho National Lab. (INL), Idaho Falls, ID (United States); Idaho State Univ., Pocatello, ID (United States); Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
  2. Idaho National Lab. (INL), Idaho Falls, ID (United States)
  3. Idaho State Univ., Pocatello, ID (United States)
  4. New Mexico Institute of Mining and Technology, Socorro, NM (United States)
Publication Date:
Report Number(s):
PNNL-SA-121820; INL/JOU-16-40289-Rev000
Journal ID: ISSN 1754-6834; PII: 1110
Grant/Contract Number:
AC05-76RL01830; AC07-05ID14517
Type:
Accepted Manuscript
Journal Name:
Biotechnology for Biofuels
Additional Journal Information:
Journal Volume: 11; Journal Issue: 1; Journal ID: ISSN 1754-6834
Publisher:
BioMed Central
Research Org:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States); Idaho National Lab. (INL), Idaho Falls, ID (United States)
Sponsoring Org:
USDOE Office of Nuclear Energy (NE)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Alicyclobacillus acidocaldarius; Wheat arabinoxylan; Glycoside hydrolase; Microarray; alicyclobacillus acidocaldarius; glycoside hydrolase gene transcription; xylan hydrolysis mechanism
OSTI Identifier:
1437038
Alternate Identifier(s):
OSTI ID: 1473709

Lee, Brady D., Apel, William A., Sheridan, Peter P., and DeVeaux, Linda C.. Glycoside hydrolase gene transcription by Alicyclobacillus acidocaldarius during growth on wheat arabinoxylan and monosaccharides: a proposed xylan hydrolysis mechanism. United States: N. p., Web. doi:10.1186/s13068-018-1110-3.
Lee, Brady D., Apel, William A., Sheridan, Peter P., & DeVeaux, Linda C.. Glycoside hydrolase gene transcription by Alicyclobacillus acidocaldarius during growth on wheat arabinoxylan and monosaccharides: a proposed xylan hydrolysis mechanism. United States. doi:10.1186/s13068-018-1110-3.
Lee, Brady D., Apel, William A., Sheridan, Peter P., and DeVeaux, Linda C.. 2018. "Glycoside hydrolase gene transcription by Alicyclobacillus acidocaldarius during growth on wheat arabinoxylan and monosaccharides: a proposed xylan hydrolysis mechanism". United States. doi:10.1186/s13068-018-1110-3. https://www.osti.gov/servlets/purl/1437038.
@article{osti_1437038,
title = {Glycoside hydrolase gene transcription by Alicyclobacillus acidocaldarius during growth on wheat arabinoxylan and monosaccharides: a proposed xylan hydrolysis mechanism},
author = {Lee, Brady D. and Apel, William A. and Sheridan, Peter P. and DeVeaux, Linda C.},
abstractNote = {Metabolism of carbon bound in wheat arabinoxylan (WAX) polysaccharides by bacteria requires a number of glycoside hydrolases active toward different bonds between sugars and other molecules. Alicyclobacillus acidocaldarius is a Gram-positive thermoacidophilic bacterium capable of growth on a variety of mono-, di-, oligo-, and polysaccharides. Nineteen proposed glycoside hydrolases have been annotated in the A. acidocaldarius Type Strain ATCC27009/DSM 446 genome. Here, experiments were performed to understand the effect of monosaccharides on gene expression during growth on the polysaccharide, WAX.},
doi = {10.1186/s13068-018-1110-3},
journal = {Biotechnology for Biofuels},
number = 1,
volume = 11,
place = {United States},
year = {2018},
month = {4}
}

Works referenced in this record:

The mechanisms of carbon catabolite repression in bacteria
journal, April 2008

Structure of endoglucanase Cel9A from the thermoacidophilic Alicyclobacillus acidocaldarius
journal, July 2009
  • Pereira, Jose Henrique; Sapra, Rajat; Volponi, Joanne V.
  • Acta Crystallographica Section D Biological Crystallography, Vol. 65, Issue 8, p. 744-750
  • DOI: 10.1107/S0907444909012773

Deconstruction of Lignocellulosic Biomass to Fuels and Chemicals
journal, July 2011

Purification, Properties and Structural Aspects of a Thermoacidophilic alpha-Amylase from Alicyclobacillus Acidocaldarius Atcc 27009
journal, December 1994

Gene cloning, sequencing, and characterization of a family 9 endoglucanase (CelA) with an unusual pattern of activity from the thermoacidophile Alicyclobacillus acidocaldarius ATCC27009
journal, December 2002
  • K., Eckert; F., Zielinski; Leggio, L. Lo
  • Applied Microbiology and Biotechnology, Vol. 60, Issue 4, p. 428-436
  • DOI: 10.1007/s00253-002-1131-4

Characterization of a β-glycosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius
journal, April 2006

Exploration, normalization, and summaries of high density oligonucleotide array probe level data
journal, April 2003

Basic local alignment search tool
journal, October 1990
  • Altschul, Stephen F.; Gish, Warren; Miller, Webb
  • Journal of Molecular Biology, Vol. 215, Issue 3, p. 403-410
  • DOI: 10.1016/S0022-2836(05)80360-2

Carbon catabolite repression in bacteria: many ways to make the most out of nutrients
journal, August 2008
  • Görke, Boris; Stülke, Jörg
  • Nature Reviews Microbiology, Vol. 6, Issue 8, p. 613-624
  • DOI: 10.1038/nrmicro1932

MUSCLE: multiple sequence alignment with high accuracy and high throughput
journal, March 2004
  • Edgar, R. C.
  • Nucleic Acids Research, Vol. 32, Issue 5, p. 1792-1797
  • DOI: 10.1093/nar/gkh340

Isolation and characterization of a new family 42 β-galactosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius: Identification of the active site residues
journal, February 2008
  • Di Lauro, Barbara; Strazzulli, Andrea; Perugino, Giuseppe
  • Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Vol. 1784, Issue 2, p. 292-301
  • DOI: 10.1016/j.bbapap.2007.10.013