Next Article in Journal
Fluorescent Reporters and Biosensors for Probing the Dynamic Behavior of Protein Kinases
Next Article in Special Issue
A Proteomic Study of Clavibacter Michiganensis Subsp. Michiganensis Culture Supernatants
Previous Article in Journal
Mitochondrial Proteomics of Antimony and Miltefosine Resistant Leishmania infantum
Article Menu

Export Article

Open AccessArticle
Proteomes 2015, 3(4), 347-368; doi:10.3390/proteomes3040347

The Cytosolic Oligosaccharide-Degrading Proteome of Butyrivibrio Proteoclasticus

1
Rumen Microbiology, Animal Science Group, AgResearch Limited, Grasslands Research Centre, Palmerston North 4442, New Zealand
2
Centre for Biodiscovery and School of Biological Sciences, Victoria University of Wellington, Wellington 6140, New Zealand
3
AgResearch Limited/Victoria University of Wellington Proteomics Laboratory, Victoria University of Wellington, Wellington 6140, New Zealand
*
Author to whom correspondence should be addressed.
Academic Editors: Michael Hecker and Katharina Riedel
Received: 31 August 2015 / Revised: 15 October 2015 / Accepted: 19 October 2015 / Published: 27 October 2015
(This article belongs to the Special Issue Microbial Proteomics)
View Full-Text   |   Download PDF [1751 KB, uploaded 27 October 2015]   |  

Abstract

The growth and productivity of ruminants depends on a complex microbial community found in their fore-stomach (rumen), which is able to breakdown plant polysaccharides and ferment the released sugars. Butyrivibrio proteoclasticus B316T is a Gram-positive polysaccharide-degrading, butyrate-producing bacterium that is present at high numbers in the rumen of animals consuming pasture or grass silage based diets. B316T is one of a small number of rumen fibrolytic microbes capable of efficiently degrading and utilizing xylan, as well as being capable of utilizing arabinose, xylose, pectin and starch. We have therefore carried out a proteomic analysis of B316T to identify intracellular enzymes that are implicated in the metabolism of internalized xylan. Three hundred and ninety four proteins were identified including enzymes that have potential to metabolize assimilated products of extracellular xylan digestion. Identified enzymes included arabinosidases, esterases, an endoxylanase, and β-xylosidase. The presence of intracellular debranching enzymes indicated that some hemicellulosic side-chains may not be removed until oligosaccharides liberated by extracellular digestion have been assimilated by the cells. The results support a model of extracellular digestion of hemicellulose to oligosaccharides that are then transported to the cytoplasm for further digestion by intracellular enzymes. View Full-Text
Keywords: butyrivibrio proteoclasticus; carbohydrate active enzymes; hemicellulose; oligosaccharidases; proteomics; rumen; xylan butyrivibrio proteoclasticus; carbohydrate active enzymes; hemicellulose; oligosaccharidases; proteomics; rumen; xylan
Figures

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Dunne, J.C.; Kelly, W.J.; Leahy, S.C.; Li, D.; Bond, J.J.; Peng, L.; Attwood, G.T.; Jordan, T.W. The Cytosolic Oligosaccharide-Degrading Proteome of Butyrivibrio Proteoclasticus. Proteomes 2015, 3, 347-368.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Proteomes EISSN 2227-7382 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top