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A functional glycogen biosynthesis pathway in Lactobacillus acidophilus: expression and analysis of the glg operon
Glycogen metabolism contributes to energy storage and various physiological functions in some prokaryotes, including colonization persistence. A role for glycogen metabolism is proposed on the survival and fitness of Lactobacillus acidophilus, a probiotic microbe, in the human gastrointestinal envir...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BlackWell Publishing Ltd
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4282360/ https://www.ncbi.nlm.nih.gov/pubmed/23879596 http://dx.doi.org/10.1111/mmi.12338 |
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author | Goh, Yong Jun Klaenhammer, Todd R |
author_facet | Goh, Yong Jun Klaenhammer, Todd R |
author_sort | Goh, Yong Jun |
collection | PubMed |
description | Glycogen metabolism contributes to energy storage and various physiological functions in some prokaryotes, including colonization persistence. A role for glycogen metabolism is proposed on the survival and fitness of Lactobacillus acidophilus, a probiotic microbe, in the human gastrointestinal environment. L. acidophilus NCFM possesses a glycogen metabolism (glg) operon consisting of glgBCDAP-amy-pgm genes. Expression of the glg operon and glycogen accumulation were carbon source- and growth phase-dependent, and were repressed by glucose. The highest intracellular glycogen content was observed in early log-phase cells grown on trehalose, which was followed by a drastic decrease of glycogen content prior to entering stationary phase. In raffinose-grown cells, however, glycogen accumulation gradually declined following early log phase and was maintained at stable levels throughout stationary phase. Raffinose also induced an overall higher temporal glg expression throughout growth compared with trehalose. Isogenic ΔglgA (glycogen synthase) and ΔglgB (glycogen-branching enzyme) mutants are glycogen-deficient and exhibited growth defects on raffinose. The latter observation suggests a reciprocal relationship between glycogen synthesis and raffinose metabolism. Deletion of glgB or glgP (glycogen phosphorylase) resulted in defective growth and increased bile sensitivity. The data indicate that glycogen metabolism is involved in growth maintenance, bile tolerance and complex carbohydrate utilization in L. acidophilus. |
format | Online Article Text |
id | pubmed-4282360 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | BlackWell Publishing Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-42823602015-01-15 A functional glycogen biosynthesis pathway in Lactobacillus acidophilus: expression and analysis of the glg operon Goh, Yong Jun Klaenhammer, Todd R Mol Microbiol Research Articles Glycogen metabolism contributes to energy storage and various physiological functions in some prokaryotes, including colonization persistence. A role for glycogen metabolism is proposed on the survival and fitness of Lactobacillus acidophilus, a probiotic microbe, in the human gastrointestinal environment. L. acidophilus NCFM possesses a glycogen metabolism (glg) operon consisting of glgBCDAP-amy-pgm genes. Expression of the glg operon and glycogen accumulation were carbon source- and growth phase-dependent, and were repressed by glucose. The highest intracellular glycogen content was observed in early log-phase cells grown on trehalose, which was followed by a drastic decrease of glycogen content prior to entering stationary phase. In raffinose-grown cells, however, glycogen accumulation gradually declined following early log phase and was maintained at stable levels throughout stationary phase. Raffinose also induced an overall higher temporal glg expression throughout growth compared with trehalose. Isogenic ΔglgA (glycogen synthase) and ΔglgB (glycogen-branching enzyme) mutants are glycogen-deficient and exhibited growth defects on raffinose. The latter observation suggests a reciprocal relationship between glycogen synthesis and raffinose metabolism. Deletion of glgB or glgP (glycogen phosphorylase) resulted in defective growth and increased bile sensitivity. The data indicate that glycogen metabolism is involved in growth maintenance, bile tolerance and complex carbohydrate utilization in L. acidophilus. BlackWell Publishing Ltd 2013-09 2013-08-16 /pmc/articles/PMC4282360/ /pubmed/23879596 http://dx.doi.org/10.1111/mmi.12338 Text en © 2013 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd. http://creativecommons.org/licenses/by/3.0/ This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Goh, Yong Jun Klaenhammer, Todd R A functional glycogen biosynthesis pathway in Lactobacillus acidophilus: expression and analysis of the glg operon |
title | A functional glycogen biosynthesis pathway in Lactobacillus acidophilus: expression and analysis of the glg operon |
title_full | A functional glycogen biosynthesis pathway in Lactobacillus acidophilus: expression and analysis of the glg operon |
title_fullStr | A functional glycogen biosynthesis pathway in Lactobacillus acidophilus: expression and analysis of the glg operon |
title_full_unstemmed | A functional glycogen biosynthesis pathway in Lactobacillus acidophilus: expression and analysis of the glg operon |
title_short | A functional glycogen biosynthesis pathway in Lactobacillus acidophilus: expression and analysis of the glg operon |
title_sort | functional glycogen biosynthesis pathway in lactobacillus acidophilus: expression and analysis of the glg operon |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4282360/ https://www.ncbi.nlm.nih.gov/pubmed/23879596 http://dx.doi.org/10.1111/mmi.12338 |
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