Loading…
Physiological Response of Corynebacterium glutamicum to Indole
The aromatic heterocyclic compound indole is widely spread in nature. Due to its floral odor indole finds application in dairy, flavor, and fragrance products. Indole is an inter- and intracellular signaling molecule influencing cell division, sporulation, or virulence in some bacteria that synthesi...
Saved in:
Published in: | Microorganisms (Basel) 2020-12, Vol.8 (12), p.1945 |
---|---|
Main Authors: | , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c505t-d7d5ed943848b232fcf4d0692cca5bf2cd86ada2719aa0f1e10ff3bcda0b21143 |
---|---|
cites | cdi_FETCH-LOGICAL-c505t-d7d5ed943848b232fcf4d0692cca5bf2cd86ada2719aa0f1e10ff3bcda0b21143 |
container_end_page | |
container_issue | 12 |
container_start_page | 1945 |
container_title | Microorganisms (Basel) |
container_volume | 8 |
creator | Walter, Tatjana Veldmann, Kareen H Götker, Susanne Busche, Tobias Rückert, Christian Kashkooli, Arman Beyraghdar Paulus, Jannik Cankar, Katarina Wendisch, Volker F |
description | The aromatic heterocyclic compound indole is widely spread in nature. Due to its floral odor indole finds application in dairy, flavor, and fragrance products. Indole is an inter- and intracellular signaling molecule influencing cell division, sporulation, or virulence in some bacteria that synthesize it from tryptophan by tryptophanase.
that is used for the industrial production of amino acids including tryptophan lacks tryptophanase. To test if indole is metabolized by
or has a regulatory role, the physiological response to indole by this bacterium was studied. As shown by RNAseq analysis, indole, which inhibited growth at low concentrations, increased expression of genes involved in the metabolism of iron, copper, and aromatic compounds. In part, this may be due to iron reduction as indole was shown to reduce Fe
to Fe
in the culture medium. Mutants with improved tolerance to indole were selected by adaptive laboratory evolution. Among the mutations identified by genome sequencing, mutations in three transcriptional regulator genes were demonstrated to be causal for increased indole tolerance. These code for the regulator of iron homeostasis DtxR, the regulator of oxidative stress response RosR, and the hitherto uncharacterized Cg3388. Gel mobility shift analysis revealed that Cg3388 binds to the intergenic region between its own gene and the
operon encoding inositol uptake system IolT2, maleylacetate reductase, and catechol 1,2-dioxygenase. Increased RNA levels of
in a
deletion strain indicated that Cg3388 acts as repressor. Indole, hydroquinone, and 1,2,4-trihydroxybenzene may function as inducers of the
operon in vivo as they interfered with DNA binding of Cg3388 at physiological concentrations in vitro. Cg3388 was named IhtR. |
doi_str_mv | 10.3390/microorganisms8121945 |
format | article |
fullrecord | <record><control><sourceid>proquest_doaj_</sourceid><recordid>TN_cdi_doaj_primary_oai_doaj_org_article_cc1cc57c33814d4e8b8b77f06c3bf270</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_cc1cc57c33814d4e8b8b77f06c3bf270</doaj_id><sourcerecordid>2473405084</sourcerecordid><originalsourceid>FETCH-LOGICAL-c505t-d7d5ed943848b232fcf4d0692cca5bf2cd86ada2719aa0f1e10ff3bcda0b21143</originalsourceid><addsrcrecordid>eNptkV1rVDEQhoMottT-BOWAN95szedJclOQxY-FgiJ6HXImyTZLzsmanCPsvzfrtqUVc5Nh8s4zk3kRek3wFWMavx8jlJzL1k6xjlURSjQXz9A5xbJf0R7L54_iM3RZ6w63owlTgrxEZ4wxTLnS5-j62-2hxpzyNoJN3Xdf93mqvsuhW-dymPxgYfYlLmO3TctsW-cWzrnbTC4n_wq9CDZVf3l3X6Cfnz7-WH9Z3Xz9vFl_uFmBwGJeOemEd5ozxdVAGQ0QuMO9pgBWDIGCU711lkqircWBeIJDYAM4iwdKCGcXaHPiumx3Zl_iaMvBZBvN30RbhbFljpC8ASAAQgJjinDHvRrUIGXAPbDWSeLGuj6x9sswegd-motNT6BPX6Z4a7b5t5Gy51KLBnh3Byj51-LrbMZYwadkJ5-XaiiXjGOB1XHut_9Id3kpU1tVU_W6V0rRI1CcVM3VWosPD8MQbI6Gm_8a3urePP7JQ9W9vewPkKasqg</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2469688825</pqid></control><display><type>article</type><title>Physiological Response of Corynebacterium glutamicum to Indole</title><source>PMC (PubMed Central)</source><source>Publicly Available Content (ProQuest)</source><creator>Walter, Tatjana ; Veldmann, Kareen H ; Götker, Susanne ; Busche, Tobias ; Rückert, Christian ; Kashkooli, Arman Beyraghdar ; Paulus, Jannik ; Cankar, Katarina ; Wendisch, Volker F</creator><creatorcontrib>Walter, Tatjana ; Veldmann, Kareen H ; Götker, Susanne ; Busche, Tobias ; Rückert, Christian ; Kashkooli, Arman Beyraghdar ; Paulus, Jannik ; Cankar, Katarina ; Wendisch, Volker F</creatorcontrib><description>The aromatic heterocyclic compound indole is widely spread in nature. Due to its floral odor indole finds application in dairy, flavor, and fragrance products. Indole is an inter- and intracellular signaling molecule influencing cell division, sporulation, or virulence in some bacteria that synthesize it from tryptophan by tryptophanase.
that is used for the industrial production of amino acids including tryptophan lacks tryptophanase. To test if indole is metabolized by
or has a regulatory role, the physiological response to indole by this bacterium was studied. As shown by RNAseq analysis, indole, which inhibited growth at low concentrations, increased expression of genes involved in the metabolism of iron, copper, and aromatic compounds. In part, this may be due to iron reduction as indole was shown to reduce Fe
to Fe
in the culture medium. Mutants with improved tolerance to indole were selected by adaptive laboratory evolution. Among the mutations identified by genome sequencing, mutations in three transcriptional regulator genes were demonstrated to be causal for increased indole tolerance. These code for the regulator of iron homeostasis DtxR, the regulator of oxidative stress response RosR, and the hitherto uncharacterized Cg3388. Gel mobility shift analysis revealed that Cg3388 binds to the intergenic region between its own gene and the
operon encoding inositol uptake system IolT2, maleylacetate reductase, and catechol 1,2-dioxygenase. Increased RNA levels of
in a
deletion strain indicated that Cg3388 acts as repressor. Indole, hydroquinone, and 1,2,4-trihydroxybenzene may function as inducers of the
operon in vivo as they interfered with DNA binding of Cg3388 at physiological concentrations in vitro. Cg3388 was named IhtR.</description><identifier>ISSN: 2076-2607</identifier><identifier>EISSN: 2076-2607</identifier><identifier>DOI: 10.3390/microorganisms8121945</identifier><identifier>PMID: 33302489</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>adaptive laboratory evolution ; Amino acids ; Antibiotics ; Aromatic compounds ; Bacteria ; Bacterial infections ; Binding sites ; Biofilms ; Catechol ; Catechol 1,2-dioxygenase ; Cell culture ; Cell division ; Copper compounds ; Corynebacterium glutamicum ; Deoxyribonucleic acid ; DNA ; E coli ; Electrophoretic mobility ; Flavor ; Flowers ; Gene expression ; Gene sequencing ; Genes ; Genomes ; Glucose ; Glycerol ; Heat resistance ; Heterocyclic compounds ; Homeostasis ; Hydroquinone ; In vivo methods and tests ; indole ; Indoles ; Industrial production ; Inositol ; Intracellular signalling ; Iron ; iron homeostasis ; Low concentrations ; Maleylacetate reductase ; Metabolism ; Mutation ; Odor ; Oxidative stress ; Physiology ; Plasmids ; Reductases ; Ribonucleic acid ; RNA ; Sporulation ; Transcription ; Tryptophan ; Tryptophan 2,3-dioxygenase ; Virulence</subject><ispartof>Microorganisms (Basel), 2020-12, Vol.8 (12), p.1945</ispartof><rights>2020. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2020 by the authors. 2020</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c505t-d7d5ed943848b232fcf4d0692cca5bf2cd86ada2719aa0f1e10ff3bcda0b21143</citedby><cites>FETCH-LOGICAL-c505t-d7d5ed943848b232fcf4d0692cca5bf2cd86ada2719aa0f1e10ff3bcda0b21143</cites><orcidid>0000-0002-6100-9135 ; 0000-0003-3473-0012</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2469688825/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2469688825?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33302489$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Walter, Tatjana</creatorcontrib><creatorcontrib>Veldmann, Kareen H</creatorcontrib><creatorcontrib>Götker, Susanne</creatorcontrib><creatorcontrib>Busche, Tobias</creatorcontrib><creatorcontrib>Rückert, Christian</creatorcontrib><creatorcontrib>Kashkooli, Arman Beyraghdar</creatorcontrib><creatorcontrib>Paulus, Jannik</creatorcontrib><creatorcontrib>Cankar, Katarina</creatorcontrib><creatorcontrib>Wendisch, Volker F</creatorcontrib><title>Physiological Response of Corynebacterium glutamicum to Indole</title><title>Microorganisms (Basel)</title><addtitle>Microorganisms</addtitle><description>The aromatic heterocyclic compound indole is widely spread in nature. Due to its floral odor indole finds application in dairy, flavor, and fragrance products. Indole is an inter- and intracellular signaling molecule influencing cell division, sporulation, or virulence in some bacteria that synthesize it from tryptophan by tryptophanase.
that is used for the industrial production of amino acids including tryptophan lacks tryptophanase. To test if indole is metabolized by
or has a regulatory role, the physiological response to indole by this bacterium was studied. As shown by RNAseq analysis, indole, which inhibited growth at low concentrations, increased expression of genes involved in the metabolism of iron, copper, and aromatic compounds. In part, this may be due to iron reduction as indole was shown to reduce Fe
to Fe
in the culture medium. Mutants with improved tolerance to indole were selected by adaptive laboratory evolution. Among the mutations identified by genome sequencing, mutations in three transcriptional regulator genes were demonstrated to be causal for increased indole tolerance. These code for the regulator of iron homeostasis DtxR, the regulator of oxidative stress response RosR, and the hitherto uncharacterized Cg3388. Gel mobility shift analysis revealed that Cg3388 binds to the intergenic region between its own gene and the
operon encoding inositol uptake system IolT2, maleylacetate reductase, and catechol 1,2-dioxygenase. Increased RNA levels of
in a
deletion strain indicated that Cg3388 acts as repressor. Indole, hydroquinone, and 1,2,4-trihydroxybenzene may function as inducers of the
operon in vivo as they interfered with DNA binding of Cg3388 at physiological concentrations in vitro. Cg3388 was named IhtR.</description><subject>adaptive laboratory evolution</subject><subject>Amino acids</subject><subject>Antibiotics</subject><subject>Aromatic compounds</subject><subject>Bacteria</subject><subject>Bacterial infections</subject><subject>Binding sites</subject><subject>Biofilms</subject><subject>Catechol</subject><subject>Catechol 1,2-dioxygenase</subject><subject>Cell culture</subject><subject>Cell division</subject><subject>Copper compounds</subject><subject>Corynebacterium glutamicum</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>E coli</subject><subject>Electrophoretic mobility</subject><subject>Flavor</subject><subject>Flowers</subject><subject>Gene expression</subject><subject>Gene sequencing</subject><subject>Genes</subject><subject>Genomes</subject><subject>Glucose</subject><subject>Glycerol</subject><subject>Heat resistance</subject><subject>Heterocyclic compounds</subject><subject>Homeostasis</subject><subject>Hydroquinone</subject><subject>In vivo methods and tests</subject><subject>indole</subject><subject>Indoles</subject><subject>Industrial production</subject><subject>Inositol</subject><subject>Intracellular signalling</subject><subject>Iron</subject><subject>iron homeostasis</subject><subject>Low concentrations</subject><subject>Maleylacetate reductase</subject><subject>Metabolism</subject><subject>Mutation</subject><subject>Odor</subject><subject>Oxidative stress</subject><subject>Physiology</subject><subject>Plasmids</subject><subject>Reductases</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>Sporulation</subject><subject>Transcription</subject><subject>Tryptophan</subject><subject>Tryptophan 2,3-dioxygenase</subject><subject>Virulence</subject><issn>2076-2607</issn><issn>2076-2607</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNptkV1rVDEQhoMottT-BOWAN95szedJclOQxY-FgiJ6HXImyTZLzsmanCPsvzfrtqUVc5Nh8s4zk3kRek3wFWMavx8jlJzL1k6xjlURSjQXz9A5xbJf0R7L54_iM3RZ6w63owlTgrxEZ4wxTLnS5-j62-2hxpzyNoJN3Xdf93mqvsuhW-dymPxgYfYlLmO3TctsW-cWzrnbTC4n_wq9CDZVf3l3X6Cfnz7-WH9Z3Xz9vFl_uFmBwGJeOemEd5ozxdVAGQ0QuMO9pgBWDIGCU711lkqircWBeIJDYAM4iwdKCGcXaHPiumx3Zl_iaMvBZBvN30RbhbFljpC8ASAAQgJjinDHvRrUIGXAPbDWSeLGuj6x9sswegd-motNT6BPX6Z4a7b5t5Gy51KLBnh3Byj51-LrbMZYwadkJ5-XaiiXjGOB1XHut_9Id3kpU1tVU_W6V0rRI1CcVM3VWosPD8MQbI6Gm_8a3urePP7JQ9W9vewPkKasqg</recordid><startdate>20201208</startdate><enddate>20201208</enddate><creator>Walter, Tatjana</creator><creator>Veldmann, Kareen H</creator><creator>Götker, Susanne</creator><creator>Busche, Tobias</creator><creator>Rückert, Christian</creator><creator>Kashkooli, Arman Beyraghdar</creator><creator>Paulus, Jannik</creator><creator>Cankar, Katarina</creator><creator>Wendisch, Volker F</creator><general>MDPI AG</general><general>MDPI</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T7</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</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>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M7P</scope><scope>P64</scope><scope>PATMY</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-6100-9135</orcidid><orcidid>https://orcid.org/0000-0003-3473-0012</orcidid></search><sort><creationdate>20201208</creationdate><title>Physiological Response of Corynebacterium glutamicum to Indole</title><author>Walter, Tatjana ; Veldmann, Kareen H ; Götker, Susanne ; Busche, Tobias ; Rückert, Christian ; Kashkooli, Arman Beyraghdar ; Paulus, Jannik ; Cankar, Katarina ; Wendisch, Volker F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c505t-d7d5ed943848b232fcf4d0692cca5bf2cd86ada2719aa0f1e10ff3bcda0b21143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>adaptive laboratory evolution</topic><topic>Amino acids</topic><topic>Antibiotics</topic><topic>Aromatic compounds</topic><topic>Bacteria</topic><topic>Bacterial infections</topic><topic>Binding sites</topic><topic>Biofilms</topic><topic>Catechol</topic><topic>Catechol 1,2-dioxygenase</topic><topic>Cell culture</topic><topic>Cell division</topic><topic>Copper compounds</topic><topic>Corynebacterium glutamicum</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>E coli</topic><topic>Electrophoretic mobility</topic><topic>Flavor</topic><topic>Flowers</topic><topic>Gene expression</topic><topic>Gene sequencing</topic><topic>Genes</topic><topic>Genomes</topic><topic>Glucose</topic><topic>Glycerol</topic><topic>Heat resistance</topic><topic>Heterocyclic compounds</topic><topic>Homeostasis</topic><topic>Hydroquinone</topic><topic>In vivo methods and tests</topic><topic>indole</topic><topic>Indoles</topic><topic>Industrial production</topic><topic>Inositol</topic><topic>Intracellular signalling</topic><topic>Iron</topic><topic>iron homeostasis</topic><topic>Low concentrations</topic><topic>Maleylacetate reductase</topic><topic>Metabolism</topic><topic>Mutation</topic><topic>Odor</topic><topic>Oxidative stress</topic><topic>Physiology</topic><topic>Plasmids</topic><topic>Reductases</topic><topic>Ribonucleic acid</topic><topic>RNA</topic><topic>Sporulation</topic><topic>Transcription</topic><topic>Tryptophan</topic><topic>Tryptophan 2,3-dioxygenase</topic><topic>Virulence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Walter, Tatjana</creatorcontrib><creatorcontrib>Veldmann, Kareen H</creatorcontrib><creatorcontrib>Götker, Susanne</creatorcontrib><creatorcontrib>Busche, Tobias</creatorcontrib><creatorcontrib>Rückert, Christian</creatorcontrib><creatorcontrib>Kashkooli, Arman Beyraghdar</creatorcontrib><creatorcontrib>Paulus, Jannik</creatorcontrib><creatorcontrib>Cankar, Katarina</creatorcontrib><creatorcontrib>Wendisch, Volker F</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Publicly Available Content (ProQuest)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Environmental Science Collection</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Microorganisms (Basel)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Walter, Tatjana</au><au>Veldmann, Kareen H</au><au>Götker, Susanne</au><au>Busche, Tobias</au><au>Rückert, Christian</au><au>Kashkooli, Arman Beyraghdar</au><au>Paulus, Jannik</au><au>Cankar, Katarina</au><au>Wendisch, Volker F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Physiological Response of Corynebacterium glutamicum to Indole</atitle><jtitle>Microorganisms (Basel)</jtitle><addtitle>Microorganisms</addtitle><date>2020-12-08</date><risdate>2020</risdate><volume>8</volume><issue>12</issue><spage>1945</spage><pages>1945-</pages><issn>2076-2607</issn><eissn>2076-2607</eissn><abstract>The aromatic heterocyclic compound indole is widely spread in nature. Due to its floral odor indole finds application in dairy, flavor, and fragrance products. Indole is an inter- and intracellular signaling molecule influencing cell division, sporulation, or virulence in some bacteria that synthesize it from tryptophan by tryptophanase.
that is used for the industrial production of amino acids including tryptophan lacks tryptophanase. To test if indole is metabolized by
or has a regulatory role, the physiological response to indole by this bacterium was studied. As shown by RNAseq analysis, indole, which inhibited growth at low concentrations, increased expression of genes involved in the metabolism of iron, copper, and aromatic compounds. In part, this may be due to iron reduction as indole was shown to reduce Fe
to Fe
in the culture medium. Mutants with improved tolerance to indole were selected by adaptive laboratory evolution. Among the mutations identified by genome sequencing, mutations in three transcriptional regulator genes were demonstrated to be causal for increased indole tolerance. These code for the regulator of iron homeostasis DtxR, the regulator of oxidative stress response RosR, and the hitherto uncharacterized Cg3388. Gel mobility shift analysis revealed that Cg3388 binds to the intergenic region between its own gene and the
operon encoding inositol uptake system IolT2, maleylacetate reductase, and catechol 1,2-dioxygenase. Increased RNA levels of
in a
deletion strain indicated that Cg3388 acts as repressor. Indole, hydroquinone, and 1,2,4-trihydroxybenzene may function as inducers of the
operon in vivo as they interfered with DNA binding of Cg3388 at physiological concentrations in vitro. Cg3388 was named IhtR.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>33302489</pmid><doi>10.3390/microorganisms8121945</doi><orcidid>https://orcid.org/0000-0002-6100-9135</orcidid><orcidid>https://orcid.org/0000-0003-3473-0012</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 2076-2607 |
ispartof | Microorganisms (Basel), 2020-12, Vol.8 (12), p.1945 |
issn | 2076-2607 2076-2607 |
language | eng |
recordid | cdi_doaj_primary_oai_doaj_org_article_cc1cc57c33814d4e8b8b77f06c3bf270 |
source | PMC (PubMed Central); Publicly Available Content (ProQuest) |
subjects | adaptive laboratory evolution Amino acids Antibiotics Aromatic compounds Bacteria Bacterial infections Binding sites Biofilms Catechol Catechol 1,2-dioxygenase Cell culture Cell division Copper compounds Corynebacterium glutamicum Deoxyribonucleic acid DNA E coli Electrophoretic mobility Flavor Flowers Gene expression Gene sequencing Genes Genomes Glucose Glycerol Heat resistance Heterocyclic compounds Homeostasis Hydroquinone In vivo methods and tests indole Indoles Industrial production Inositol Intracellular signalling Iron iron homeostasis Low concentrations Maleylacetate reductase Metabolism Mutation Odor Oxidative stress Physiology Plasmids Reductases Ribonucleic acid RNA Sporulation Transcription Tryptophan Tryptophan 2,3-dioxygenase Virulence |
title | Physiological Response of Corynebacterium glutamicum to Indole |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-30T22%3A47%3A48IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_doaj_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Physiological%20Response%20of%20Corynebacterium%20glutamicum%20to%20Indole&rft.jtitle=Microorganisms%20(Basel)&rft.au=Walter,%20Tatjana&rft.date=2020-12-08&rft.volume=8&rft.issue=12&rft.spage=1945&rft.pages=1945-&rft.issn=2076-2607&rft.eissn=2076-2607&rft_id=info:doi/10.3390/microorganisms8121945&rft_dat=%3Cproquest_doaj_%3E2473405084%3C/proquest_doaj_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c505t-d7d5ed943848b232fcf4d0692cca5bf2cd86ada2719aa0f1e10ff3bcda0b21143%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2469688825&rft_id=info:pmid/33302489&rfr_iscdi=true |