Protein PII regulates both inorganic carbon and nitrate uptake and is modified by a redox signal in Synechocystis PCC 6803
In Synechocystis PCC 6803 as in other cyanobacteria, involvement of protein PII in the co-regulation of inorganic carbon and nitrogen metabolism was established based on post-translational modifications of the protein resulting from changes in the carbon/nitrogen regimes. Uptake of bicarbonate and n...
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| Veröffentlicht in: | FEBS letters 1999-12, Vol.463 (3), p.216-220 |
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| container_title | FEBS letters |
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| creator | Hisbergues, Michael Jeanjean, Robert Joset, Françoise Tandeau de Marsac, Nicole Bédu, Sylvie |
| description | In
Synechocystis PCC 6803 as in other cyanobacteria, involvement of protein PII in the co-regulation of inorganic carbon and nitrogen metabolism was established based on post-translational modifications of the protein resulting from changes in the carbon/nitrogen regimes. Uptake of bicarbonate and nitrate in response to changes of the carbon and/or nitrogen regimes is altered in a PII-null mutant, indicating that both processes are under control of PII. Modulation of electron flow by addition of methyl viologen with or without duroquinol, or in a NAD(P)H dehydrogenase-deficient mutant, affects the phosphorylation level of PII. The redox state of the cells would thus act as a trigger for PII phosphorylation. |
| doi_str_mv | 10.1016/S0014-5793(99)01624-5 |
| format | Article |
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Synechocystis PCC 6803 as in other cyanobacteria, involvement of protein PII in the co-regulation of inorganic carbon and nitrogen metabolism was established based on post-translational modifications of the protein resulting from changes in the carbon/nitrogen regimes. Uptake of bicarbonate and nitrate in response to changes of the carbon and/or nitrogen regimes is altered in a PII-null mutant, indicating that both processes are under control of PII. Modulation of electron flow by addition of methyl viologen with or without duroquinol, or in a NAD(P)H dehydrogenase-deficient mutant, affects the phosphorylation level of PII. The redox state of the cells would thus act as a trigger for PII phosphorylation.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(99)01624-5</identifier><identifier>PMID: 10606724</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Bacterial Proteins - genetics ; Bacterial Proteins - pharmacology ; Bicarbonate uptake ; Bicarbonates - metabolism ; Cyanobacteria - drug effects ; Cyanobacteria - genetics ; Cyanobacteria - metabolism ; Cyanobacterium ; Hydroquinones ; NADPH Dehydrogenase - deficiency ; NADPH Dehydrogenase - genetics ; Nitrate uptake ; Nitrates - metabolism ; Oxidation-Reduction ; Paraquat ; Phosphorylation ; PII Nitrogen Regulatory Proteins ; Protein Kinases - metabolism ; Protein PII ; Redox state</subject><ispartof>FEBS letters, 1999-12, Vol.463 (3), p.216-220</ispartof><rights>1999 Federation of European Biochemical Societies</rights><rights>FEBS Letters 463 (1999) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4265-54d6431ee159a92f812f33d4325a889f10c6dcafe8d33dc137eb9fb1edc56b693</citedby><cites>FETCH-LOGICAL-c4265-54d6431ee159a92f812f33d4325a889f10c6dcafe8d33dc137eb9fb1edc56b693</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2899%2901624-5$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579399016245$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10606724$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hisbergues, Michael</creatorcontrib><creatorcontrib>Jeanjean, Robert</creatorcontrib><creatorcontrib>Joset, Françoise</creatorcontrib><creatorcontrib>Tandeau de Marsac, Nicole</creatorcontrib><creatorcontrib>Bédu, Sylvie</creatorcontrib><title>Protein PII regulates both inorganic carbon and nitrate uptake and is modified by a redox signal in Synechocystis PCC 6803</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>In
Synechocystis PCC 6803 as in other cyanobacteria, involvement of protein PII in the co-regulation of inorganic carbon and nitrogen metabolism was established based on post-translational modifications of the protein resulting from changes in the carbon/nitrogen regimes. Uptake of bicarbonate and nitrate in response to changes of the carbon and/or nitrogen regimes is altered in a PII-null mutant, indicating that both processes are under control of PII. Modulation of electron flow by addition of methyl viologen with or without duroquinol, or in a NAD(P)H dehydrogenase-deficient mutant, affects the phosphorylation level of PII. The redox state of the cells would thus act as a trigger for PII phosphorylation.</description><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - pharmacology</subject><subject>Bicarbonate uptake</subject><subject>Bicarbonates - metabolism</subject><subject>Cyanobacteria - drug effects</subject><subject>Cyanobacteria - genetics</subject><subject>Cyanobacteria - metabolism</subject><subject>Cyanobacterium</subject><subject>Hydroquinones</subject><subject>NADPH Dehydrogenase - deficiency</subject><subject>NADPH Dehydrogenase - genetics</subject><subject>Nitrate uptake</subject><subject>Nitrates - metabolism</subject><subject>Oxidation-Reduction</subject><subject>Paraquat</subject><subject>Phosphorylation</subject><subject>PII Nitrogen Regulatory Proteins</subject><subject>Protein Kinases - metabolism</subject><subject>Protein PII</subject><subject>Redox state</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEFP3DAQhS1UBAvtT2jlU0UPoXacOPGpghWUlZC6Eu3ZcuzJ4jZrb-0EGn59vQlCvdHTaN5882b0EHpPyTkllH--I4QWWVkJdibEp6TkqTtAC1pXLGMFr9-gxQtyjE5i_ElSX1NxhI4p4YRXebFAT-vge7AOr1crHGAzdKqHiBvf32PrfNgoZzXWKjTeYeUMdrYPCcHDrle_YJJsxFtvbGvB4GbEKvkY_wdHu3GqSy74bnSg770eY5_Y9XKJeU3YW3TYqi7Cu-d6in5cX31f3mS3376ulhe3mS5yXmZlYXjBKAAthRJ5W9O8ZcwULC9VXYuWEs2NVi3UJsmasgoa0TYUjC55wwU7RR9n313wvweIvdzaqKHrlAM_RJkQLvKKJLCcQR18jAFauQt2q8IoKZH70OUUutwnKoWQU-iyTHsfng8MzRbMP1tzygm4mYFH28H4f67y-uoynyb7gRCTvL_1ZbaClNiDhSCjtuA0GBtA99J4-8q3fwFb76Vj</recordid><startdate>19991217</startdate><enddate>19991217</enddate><creator>Hisbergues, Michael</creator><creator>Jeanjean, Robert</creator><creator>Joset, Françoise</creator><creator>Tandeau de Marsac, Nicole</creator><creator>Bédu, Sylvie</creator><general>Elsevier B.V</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>7X8</scope></search><sort><creationdate>19991217</creationdate><title>Protein PII regulates both inorganic carbon and nitrate uptake and is modified by a redox signal in Synechocystis PCC 6803</title><author>Hisbergues, Michael ; Jeanjean, Robert ; Joset, Françoise ; Tandeau de Marsac, Nicole ; Bédu, Sylvie</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4265-54d6431ee159a92f812f33d4325a889f10c6dcafe8d33dc137eb9fb1edc56b693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - pharmacology</topic><topic>Bicarbonate uptake</topic><topic>Bicarbonates - metabolism</topic><topic>Cyanobacteria - drug effects</topic><topic>Cyanobacteria - genetics</topic><topic>Cyanobacteria - metabolism</topic><topic>Cyanobacterium</topic><topic>Hydroquinones</topic><topic>NADPH Dehydrogenase - deficiency</topic><topic>NADPH Dehydrogenase - genetics</topic><topic>Nitrate uptake</topic><topic>Nitrates - metabolism</topic><topic>Oxidation-Reduction</topic><topic>Paraquat</topic><topic>Phosphorylation</topic><topic>PII Nitrogen Regulatory Proteins</topic><topic>Protein Kinases - metabolism</topic><topic>Protein PII</topic><topic>Redox state</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hisbergues, Michael</creatorcontrib><creatorcontrib>Jeanjean, Robert</creatorcontrib><creatorcontrib>Joset, Françoise</creatorcontrib><creatorcontrib>Tandeau de Marsac, Nicole</creatorcontrib><creatorcontrib>Bédu, Sylvie</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>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hisbergues, Michael</au><au>Jeanjean, Robert</au><au>Joset, Françoise</au><au>Tandeau de Marsac, Nicole</au><au>Bédu, Sylvie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein PII regulates both inorganic carbon and nitrate uptake and is modified by a redox signal in Synechocystis PCC 6803</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1999-12-17</date><risdate>1999</risdate><volume>463</volume><issue>3</issue><spage>216</spage><epage>220</epage><pages>216-220</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>In
Synechocystis PCC 6803 as in other cyanobacteria, involvement of protein PII in the co-regulation of inorganic carbon and nitrogen metabolism was established based on post-translational modifications of the protein resulting from changes in the carbon/nitrogen regimes. Uptake of bicarbonate and nitrate in response to changes of the carbon and/or nitrogen regimes is altered in a PII-null mutant, indicating that both processes are under control of PII. Modulation of electron flow by addition of methyl viologen with or without duroquinol, or in a NAD(P)H dehydrogenase-deficient mutant, affects the phosphorylation level of PII. The redox state of the cells would thus act as a trigger for PII phosphorylation.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>10606724</pmid><doi>10.1016/S0014-5793(99)01624-5</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1999-12, Vol.463 (3), p.216-220 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Bacterial Proteins - genetics Bacterial Proteins - pharmacology Bicarbonate uptake Bicarbonates - metabolism Cyanobacteria - drug effects Cyanobacteria - genetics Cyanobacteria - metabolism Cyanobacterium Hydroquinones NADPH Dehydrogenase - deficiency NADPH Dehydrogenase - genetics Nitrate uptake Nitrates - metabolism Oxidation-Reduction Paraquat Phosphorylation PII Nitrogen Regulatory Proteins Protein Kinases - metabolism Protein PII Redox state |
| title | Protein PII regulates both inorganic carbon and nitrate uptake and is modified by a redox signal in Synechocystis PCC 6803 |
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