The role of GlnD in ammonia assimilation in Mycobacterium tuberculosis
Summary The control of ammonia assimilation in Mycobacterium tuberculosis is poorly understood. We have been investigating a regulatory cascade predicted to control the activity of glutamine synthetase (GS). We previously demonstrated that the GS-modifying protein, GlnE (an adenylyl transferase), is...
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| Veröffentlicht in: | Tuberculosis (Edinburgh, Scotland) Scotland), 2007-07, Vol.87 (4), p.384-390 |
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| creator | Read, Rose Pashley, Carey A Smith, Debbie Parish, Tanya |
| description | Summary The control of ammonia assimilation in Mycobacterium tuberculosis is poorly understood. We have been investigating a regulatory cascade predicted to control the activity of glutamine synthetase (GS). We previously demonstrated that the GS-modifying protein, GlnE (an adenylyl transferase), is essential for M. tuberculosis growth. GlnD, a uridylyl transferase, is involved in the control of GlnE activity in other bacteria. In M. tuberculosis , glnD is arranged in an apparent operon with amt and glnB ; all three genes are up-regulated in a low-ammonia medium. We constructed an in-frame deletion of glnD by homologous recombination. The mutant had no growth defect in media containing different nitrogen sources. Total GS activity in culture filtrates was markedly reduced in the mutant, although activity in cell-free extracts remained normal. Virulence was unaffected in both in vitro and in vivo model systems of infection, indicating that the presence of extra-cellular GS is not critical for virulence and that the residual intra-cellular GS activity is sufficient. Thus although GlnD does play a role in the control of ammonia assimilation, it is not required for virulence. |
| doi_str_mv | 10.1016/j.tube.2006.12.003 |
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We have been investigating a regulatory cascade predicted to control the activity of glutamine synthetase (GS). We previously demonstrated that the GS-modifying protein, GlnE (an adenylyl transferase), is essential for M. tuberculosis growth. GlnD, a uridylyl transferase, is involved in the control of GlnE activity in other bacteria. In M. tuberculosis , glnD is arranged in an apparent operon with amt and glnB ; all three genes are up-regulated in a low-ammonia medium. We constructed an in-frame deletion of glnD by homologous recombination. The mutant had no growth defect in media containing different nitrogen sources. Total GS activity in culture filtrates was markedly reduced in the mutant, although activity in cell-free extracts remained normal. Virulence was unaffected in both in vitro and in vivo model systems of infection, indicating that the presence of extra-cellular GS is not critical for virulence and that the residual intra-cellular GS activity is sufficient. Thus although GlnD does play a role in the control of ammonia assimilation, it is not required for virulence.</description><identifier>ISSN: 1472-9792</identifier><identifier>EISSN: 1873-281X</identifier><identifier>DOI: 10.1016/j.tube.2006.12.003</identifier><identifier>PMID: 17303474</identifier><language>eng</language><publisher>Scotland: Elsevier Ltd</publisher><subject>Ammonia - metabolism ; Animals ; Catalysis ; Gene regulation ; Genes, Bacterial - physiology ; Glutamate-Ammonia Ligase - metabolism ; Glutamine synthetase ; In Vitro Techniques ; Infectious Disease ; Macrophages - microbiology ; Mice ; Mice, SCID ; Mutant Proteins ; Mycobacterium tuberculosis ; Mycobacterium tuberculosis - genetics ; Mycobacterium tuberculosis - metabolism ; Nitrogen metabolism ; Protein Processing, Post-Translational ; Pulmonary/Respiratory ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Deletion ; Virulence</subject><ispartof>Tuberculosis (Edinburgh, Scotland), 2007-07, Vol.87 (4), p.384-390</ispartof><rights>Elsevier Ltd</rights><rights>2007 Elsevier Ltd</rights><rights>2007 Elsevier Ltd. 2007 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c539t-f16285118930fd9cb23973ffc3d2b11add089e930d7dbea493526c7f8e85ebdd3</citedby><cites>FETCH-LOGICAL-c539t-f16285118930fd9cb23973ffc3d2b11add089e930d7dbea493526c7f8e85ebdd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.tube.2006.12.003$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17303474$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Read, Rose</creatorcontrib><creatorcontrib>Pashley, Carey A</creatorcontrib><creatorcontrib>Smith, Debbie</creatorcontrib><creatorcontrib>Parish, Tanya</creatorcontrib><title>The role of GlnD in ammonia assimilation in Mycobacterium tuberculosis</title><title>Tuberculosis (Edinburgh, Scotland)</title><addtitle>Tuberculosis (Edinb)</addtitle><description>Summary The control of ammonia assimilation in Mycobacterium tuberculosis is poorly understood. We have been investigating a regulatory cascade predicted to control the activity of glutamine synthetase (GS). We previously demonstrated that the GS-modifying protein, GlnE (an adenylyl transferase), is essential for M. tuberculosis growth. GlnD, a uridylyl transferase, is involved in the control of GlnE activity in other bacteria. In M. tuberculosis , glnD is arranged in an apparent operon with amt and glnB ; all three genes are up-regulated in a low-ammonia medium. We constructed an in-frame deletion of glnD by homologous recombination. The mutant had no growth defect in media containing different nitrogen sources. Total GS activity in culture filtrates was markedly reduced in the mutant, although activity in cell-free extracts remained normal. Virulence was unaffected in both in vitro and in vivo model systems of infection, indicating that the presence of extra-cellular GS is not critical for virulence and that the residual intra-cellular GS activity is sufficient. Thus although GlnD does play a role in the control of ammonia assimilation, it is not required for virulence.</description><subject>Ammonia - metabolism</subject><subject>Animals</subject><subject>Catalysis</subject><subject>Gene regulation</subject><subject>Genes, Bacterial - physiology</subject><subject>Glutamate-Ammonia Ligase - metabolism</subject><subject>Glutamine synthetase</subject><subject>In Vitro Techniques</subject><subject>Infectious Disease</subject><subject>Macrophages - microbiology</subject><subject>Mice</subject><subject>Mice, SCID</subject><subject>Mutant Proteins</subject><subject>Mycobacterium tuberculosis</subject><subject>Mycobacterium tuberculosis - genetics</subject><subject>Mycobacterium tuberculosis - metabolism</subject><subject>Nitrogen metabolism</subject><subject>Protein Processing, Post-Translational</subject><subject>Pulmonary/Respiratory</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Sequence Deletion</subject><subject>Virulence</subject><issn>1472-9792</issn><issn>1873-281X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUk1v1TAQjBCIfsAf4IBy4pbgtZM4llAl1NIWqaiHFomb5dgb6odjFzup9P49jt4T0B7g5JV3ZuzdmaJ4A6QGAt37TT0vA9aUkK4GWhPCnhWH0HNW0R6-Pc91w2kluKAHxVFKG5JJpCcviwPgjLCGN4fF-e0dljE4LMNYXjh_VlpfqmkK3qpSpWQn69Rsg1_vv2x1GJSeMdplKtfHo15cSDa9Kl6MyiV8vT-Pi6_nn25PL6ur64vPpx-vKt0yMVcjdLRvAXrByGiEHigTnI2jZoYOAMoY0gvMTcPNgKoRrKWd5mOPfYuDMey4ONnp3i_DhEajn6Ny8j7aScWtDMrKxx1v7-T38CBBAMu6WeDdXiCGnwumWU42aXROeQxLkpx0LSct_S8QREfapoUMpDugjiGliOPv3wCRq09yI9dVydUnCVRmnzLp7d9z_KHsjcmADzsA5m0-WIwyaYteo7ER9SxNsP_WP3lC1856q5X7gVtMm7BEn32SIFMmyJs1KWtQSJdDQiljvwCVdbpe</recordid><startdate>20070701</startdate><enddate>20070701</enddate><creator>Read, Rose</creator><creator>Pashley, Carey A</creator><creator>Smith, Debbie</creator><creator>Parish, Tanya</creator><general>Elsevier Ltd</general><general>Churchill Livingstone</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20070701</creationdate><title>The role of GlnD in ammonia assimilation in Mycobacterium tuberculosis</title><author>Read, Rose ; Pashley, Carey A ; Smith, Debbie ; Parish, Tanya</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c539t-f16285118930fd9cb23973ffc3d2b11add089e930d7dbea493526c7f8e85ebdd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Ammonia - metabolism</topic><topic>Animals</topic><topic>Catalysis</topic><topic>Gene regulation</topic><topic>Genes, Bacterial - physiology</topic><topic>Glutamate-Ammonia Ligase - metabolism</topic><topic>Glutamine synthetase</topic><topic>In Vitro Techniques</topic><topic>Infectious Disease</topic><topic>Macrophages - microbiology</topic><topic>Mice</topic><topic>Mice, SCID</topic><topic>Mutant Proteins</topic><topic>Mycobacterium tuberculosis</topic><topic>Mycobacterium tuberculosis - genetics</topic><topic>Mycobacterium tuberculosis - metabolism</topic><topic>Nitrogen metabolism</topic><topic>Protein Processing, Post-Translational</topic><topic>Pulmonary/Respiratory</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Sequence Deletion</topic><topic>Virulence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Read, Rose</creatorcontrib><creatorcontrib>Pashley, Carey A</creatorcontrib><creatorcontrib>Smith, Debbie</creatorcontrib><creatorcontrib>Parish, Tanya</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Tuberculosis (Edinburgh, Scotland)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Read, Rose</au><au>Pashley, Carey A</au><au>Smith, Debbie</au><au>Parish, Tanya</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The role of GlnD in ammonia assimilation in Mycobacterium tuberculosis</atitle><jtitle>Tuberculosis (Edinburgh, Scotland)</jtitle><addtitle>Tuberculosis (Edinb)</addtitle><date>2007-07-01</date><risdate>2007</risdate><volume>87</volume><issue>4</issue><spage>384</spage><epage>390</epage><pages>384-390</pages><issn>1472-9792</issn><eissn>1873-281X</eissn><abstract>Summary The control of ammonia assimilation in Mycobacterium tuberculosis is poorly understood. We have been investigating a regulatory cascade predicted to control the activity of glutamine synthetase (GS). We previously demonstrated that the GS-modifying protein, GlnE (an adenylyl transferase), is essential for M. tuberculosis growth. GlnD, a uridylyl transferase, is involved in the control of GlnE activity in other bacteria. In M. tuberculosis , glnD is arranged in an apparent operon with amt and glnB ; all three genes are up-regulated in a low-ammonia medium. We constructed an in-frame deletion of glnD by homologous recombination. The mutant had no growth defect in media containing different nitrogen sources. Total GS activity in culture filtrates was markedly reduced in the mutant, although activity in cell-free extracts remained normal. Virulence was unaffected in both in vitro and in vivo model systems of infection, indicating that the presence of extra-cellular GS is not critical for virulence and that the residual intra-cellular GS activity is sufficient. Thus although GlnD does play a role in the control of ammonia assimilation, it is not required for virulence.</abstract><cop>Scotland</cop><pub>Elsevier Ltd</pub><pmid>17303474</pmid><doi>10.1016/j.tube.2006.12.003</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Ammonia - metabolism Animals Catalysis Gene regulation Genes, Bacterial - physiology Glutamate-Ammonia Ligase - metabolism Glutamine synthetase In Vitro Techniques Infectious Disease Macrophages - microbiology Mice Mice, SCID Mutant Proteins Mycobacterium tuberculosis Mycobacterium tuberculosis - genetics Mycobacterium tuberculosis - metabolism Nitrogen metabolism Protein Processing, Post-Translational Pulmonary/Respiratory Reverse Transcriptase Polymerase Chain Reaction Sequence Deletion Virulence |
| title | The role of GlnD in ammonia assimilation in Mycobacterium tuberculosis |
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