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Analysis of genes involved in glycogen degradation in Escherichia coli
Abstract Escherichia coli accumulate or degrade glycogen depending on environmental carbon supply. Glycogen phosphorylase (GlgP) and glycogen debranching enzyme (GlgX) are known to act on the glycogen polymer, while maltodextrin phosphorylase (MalP) is thought to remove maltodextrins released by Glg...
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| Published in: | FEMS microbiology letters 2017-02, Vol.364 (3), p.fnx016 |
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| Main Authors: | , , , , , , , |
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| container_issue | 3 |
| container_start_page | fnx016 |
| container_title | FEMS microbiology letters |
| container_volume | 364 |
| creator | Strydom, Lindi Jewell, Jonathan Meier, Michael A. George, Gavin M. Pfister, Barbara Zeeman, Samuel Kossmann, Jens Lloyd, James R. |
| description | Abstract
Escherichia coli accumulate or degrade glycogen depending on environmental carbon supply. Glycogen phosphorylase (GlgP) and glycogen debranching enzyme (GlgX) are known to act on the glycogen polymer, while maltodextrin phosphorylase (MalP) is thought to remove maltodextrins released by GlgX. To examine the roles of these enzymes in more detail, single, double and triple mutants lacking all their activities were produced. GlgX and GlgP were shown to act directly on the glycogen polymer, while MalP most likely catabolised soluble malto-oligosaccharides. Interestingly, analysis of a triple mutant lacking all three enzymes indicates the presence of another enzyme that can release maltodextrins from glycogen.
Analysis of Escherichia coli lacking combinations of MalP, GlgX and GlgP indicates that they are all involved in glycogen degradation. |
| doi_str_mv | 10.1093/femsle/fnx016 |
| format | article |
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Escherichia coli accumulate or degrade glycogen depending on environmental carbon supply. Glycogen phosphorylase (GlgP) and glycogen debranching enzyme (GlgX) are known to act on the glycogen polymer, while maltodextrin phosphorylase (MalP) is thought to remove maltodextrins released by GlgX. To examine the roles of these enzymes in more detail, single, double and triple mutants lacking all their activities were produced. GlgX and GlgP were shown to act directly on the glycogen polymer, while MalP most likely catabolised soluble malto-oligosaccharides. Interestingly, analysis of a triple mutant lacking all three enzymes indicates the presence of another enzyme that can release maltodextrins from glycogen.
Analysis of Escherichia coli lacking combinations of MalP, GlgX and GlgP indicates that they are all involved in glycogen degradation.</description><identifier>ISSN: 1574-6968</identifier><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1093/femsle/fnx016</identifier><identifier>PMID: 28119371</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Bacteria ; Coliforms ; Degradation ; E coli ; Enzymes ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Genes, Bacterial ; Glucosyltransferases - genetics ; Glucosyltransferases - metabolism ; Glycogen ; Glycogen - metabolism ; Glycogen Debranching Enzyme System - genetics ; Glycogen phosphorylase ; Glycogen Phosphorylase - genetics ; Glycogen Phosphorylase - metabolism ; Maltodextrin ; Maltodextrin phosphorylase ; Microbiology ; Oligosaccharides ; Phosphorylase ; Polymers ; Polysaccharides - metabolism</subject><ispartof>FEMS microbiology letters, 2017-02, Vol.364 (3), p.fnx016</ispartof><rights>FEMS 2017. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com 2017</rights><rights>FEMS 2017. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.</rights><rights>Copyright Oxford University Press, UK Feb 2017</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c393t-f4cdfdb5fc6caec6c666fbb79fdcfe0f30d61383336ac6b3bf0415d7c1f01773</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28119371$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Strydom, Lindi</creatorcontrib><creatorcontrib>Jewell, Jonathan</creatorcontrib><creatorcontrib>Meier, Michael A.</creatorcontrib><creatorcontrib>George, Gavin M.</creatorcontrib><creatorcontrib>Pfister, Barbara</creatorcontrib><creatorcontrib>Zeeman, Samuel</creatorcontrib><creatorcontrib>Kossmann, Jens</creatorcontrib><creatorcontrib>Lloyd, James R.</creatorcontrib><title>Analysis of genes involved in glycogen degradation in Escherichia coli</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
Escherichia coli accumulate or degrade glycogen depending on environmental carbon supply. Glycogen phosphorylase (GlgP) and glycogen debranching enzyme (GlgX) are known to act on the glycogen polymer, while maltodextrin phosphorylase (MalP) is thought to remove maltodextrins released by GlgX. To examine the roles of these enzymes in more detail, single, double and triple mutants lacking all their activities were produced. GlgX and GlgP were shown to act directly on the glycogen polymer, while MalP most likely catabolised soluble malto-oligosaccharides. Interestingly, analysis of a triple mutant lacking all three enzymes indicates the presence of another enzyme that can release maltodextrins from glycogen.
Analysis of Escherichia coli lacking combinations of MalP, GlgX and GlgP indicates that they are all involved in glycogen degradation.</description><subject>Bacteria</subject><subject>Coliforms</subject><subject>Degradation</subject><subject>E coli</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Genes, Bacterial</subject><subject>Glucosyltransferases - genetics</subject><subject>Glucosyltransferases - metabolism</subject><subject>Glycogen</subject><subject>Glycogen - metabolism</subject><subject>Glycogen Debranching Enzyme System - genetics</subject><subject>Glycogen phosphorylase</subject><subject>Glycogen Phosphorylase - genetics</subject><subject>Glycogen Phosphorylase - metabolism</subject><subject>Maltodextrin</subject><subject>Maltodextrin phosphorylase</subject><subject>Microbiology</subject><subject>Oligosaccharides</subject><subject>Phosphorylase</subject><subject>Polymers</subject><subject>Polysaccharides - metabolism</subject><issn>1574-6968</issn><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNqFkD1PwzAQhi0EoqUwsqJILCyhvjhxkrGqWkCqxNLdcvzRunLiYjcV_fdNlfIhFpa70-nRq7sHoXvAz4BLMtaqDlaNdfOJgV6gIWR5GtOSFpe_5gG6CWGDMU4TTK_RICkASpLDEM0nDbeHYELkdLRSjQqRafbO7pXshmhlD8J160iqleeS74xrTvtZEGvljVgbHglnzS260twGdXfuI7Scz5bT13jx_vI2nSxiQUqyi3UqpJZVpgUVXHWFUqqrKi-1FFphTbCkQApCCOWCVqTSOIVM5gI0hjwnI_TUx269-2hV2LHaBKGs5Y1ybWBQUCgyKOkJffyDblzru2cDSzoPWZEQXHRU3FPCuxC80mzrTc39gQFmJ7-s98t6vx3_cE5tq1rJb_pL6M-Frt3-k3UEKpGGjQ</recordid><startdate>20170201</startdate><enddate>20170201</enddate><creator>Strydom, Lindi</creator><creator>Jewell, Jonathan</creator><creator>Meier, Michael A.</creator><creator>George, Gavin M.</creator><creator>Pfister, Barbara</creator><creator>Zeeman, Samuel</creator><creator>Kossmann, Jens</creator><creator>Lloyd, James R.</creator><general>Oxford University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20170201</creationdate><title>Analysis of genes involved in glycogen degradation in Escherichia coli</title><author>Strydom, Lindi ; Jewell, Jonathan ; Meier, Michael A. ; George, Gavin M. ; Pfister, Barbara ; Zeeman, Samuel ; Kossmann, Jens ; Lloyd, James R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-f4cdfdb5fc6caec6c666fbb79fdcfe0f30d61383336ac6b3bf0415d7c1f01773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Bacteria</topic><topic>Coliforms</topic><topic>Degradation</topic><topic>E coli</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Genes, Bacterial</topic><topic>Glucosyltransferases - genetics</topic><topic>Glucosyltransferases - metabolism</topic><topic>Glycogen</topic><topic>Glycogen - metabolism</topic><topic>Glycogen Debranching Enzyme System - genetics</topic><topic>Glycogen phosphorylase</topic><topic>Glycogen Phosphorylase - genetics</topic><topic>Glycogen Phosphorylase - metabolism</topic><topic>Maltodextrin</topic><topic>Maltodextrin phosphorylase</topic><topic>Microbiology</topic><topic>Oligosaccharides</topic><topic>Phosphorylase</topic><topic>Polymers</topic><topic>Polysaccharides - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Strydom, Lindi</creatorcontrib><creatorcontrib>Jewell, Jonathan</creatorcontrib><creatorcontrib>Meier, Michael A.</creatorcontrib><creatorcontrib>George, Gavin M.</creatorcontrib><creatorcontrib>Pfister, Barbara</creatorcontrib><creatorcontrib>Zeeman, Samuel</creatorcontrib><creatorcontrib>Kossmann, Jens</creatorcontrib><creatorcontrib>Lloyd, James R.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Strydom, Lindi</au><au>Jewell, Jonathan</au><au>Meier, Michael A.</au><au>George, Gavin M.</au><au>Pfister, Barbara</au><au>Zeeman, Samuel</au><au>Kossmann, Jens</au><au>Lloyd, James R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of genes involved in glycogen degradation in Escherichia coli</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2017-02-01</date><risdate>2017</risdate><volume>364</volume><issue>3</issue><spage>fnx016</spage><pages>fnx016-</pages><issn>1574-6968</issn><issn>0378-1097</issn><eissn>1574-6968</eissn><abstract>Abstract
Escherichia coli accumulate or degrade glycogen depending on environmental carbon supply. Glycogen phosphorylase (GlgP) and glycogen debranching enzyme (GlgX) are known to act on the glycogen polymer, while maltodextrin phosphorylase (MalP) is thought to remove maltodextrins released by GlgX. To examine the roles of these enzymes in more detail, single, double and triple mutants lacking all their activities were produced. GlgX and GlgP were shown to act directly on the glycogen polymer, while MalP most likely catabolised soluble malto-oligosaccharides. Interestingly, analysis of a triple mutant lacking all three enzymes indicates the presence of another enzyme that can release maltodextrins from glycogen.
Analysis of Escherichia coli lacking combinations of MalP, GlgX and GlgP indicates that they are all involved in glycogen degradation.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>28119371</pmid><doi>10.1093/femsle/fnx016</doi><oa>free_for_read</oa></addata></record> |
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| ispartof | FEMS microbiology letters, 2017-02, Vol.364 (3), p.fnx016 |
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| language | eng |
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| source | Oxford University Press:Jisc Collections:OUP Read and Publish 2024-2025 (2024 collection) (Reading list) |
| subjects | Bacteria Coliforms Degradation E coli Enzymes Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Genes, Bacterial Glucosyltransferases - genetics Glucosyltransferases - metabolism Glycogen Glycogen - metabolism Glycogen Debranching Enzyme System - genetics Glycogen phosphorylase Glycogen Phosphorylase - genetics Glycogen Phosphorylase - metabolism Maltodextrin Maltodextrin phosphorylase Microbiology Oligosaccharides Phosphorylase Polymers Polysaccharides - metabolism |
| title | Analysis of genes involved in glycogen degradation in Escherichia coli |
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