CcbP, a Calcium-Binding Protein from Anabaena sp. PCC 7120, Provides Evidence That Calcium Ions Regulate Heterocyst Differentiation
Although it is known that calcium is a very important messenger involved in many eukaryotic cellular processes, much less is known about calcium's role in bacteria. CcbP, a Ca2+-binding protein, was isolated from the heterocystous cyanobacterium Anabaena sp. PCC 7120, and the ccbP gene was clon...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2005-04, Vol.102 (16), p.5744-5748 |
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| creator | Zhao, Yinhong Shi, Yunming Zhao, Weixing Huang, Xu Wang, Donghui Brown, Neil Brand, Jerry Zhao, Jindong Haselkorn, Robert |
| description | Although it is known that calcium is a very important messenger involved in many eukaryotic cellular processes, much less is known about calcium's role in bacteria. CcbP, a Ca2+-binding protein, was isolated from the heterocystous cyanobacterium Anabaena sp. PCC 7120, and the ccbP gene was cloned and inactivated. In the absence of combined nitrogen, inactivation of ccbP resulted in multiple contiguous heterocysts, whereas overexpression of ccbP suppressed heterocyst formation. Calmodulin, which is not present in Anabaena species, could also suppress heterocyst formation in both Anabaena sp. PCC 7120 and Anabaena variabilis. HetR induction upon nitrogen step-down was slow in the strain overexpressing ccbP. The Ca2+reporter protein obelin was used to show that mature heterocysts had a high intracellular free Ca2+concentration {[ Ca2+]i}, and immunoblotting showed that CcbP was absent from heterocysts. A regular pattern of cells with higher [ Ca2+]iwas established during heterocyst differentiation before the appearance of proheterocysts. A rapid increase of [ Ca2+]icould be detected 4 h after the removal of combined nitrogen, and this increase was suppressed by excessive CcbP. These results suggest that Ca2+ions play very important roles in hetR induction and heterocyst differentiation. |
| doi_str_mv | 10.1073/pnas.0501782102 |
| format | Article |
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PCC 7120, Provides Evidence That Calcium Ions Regulate Heterocyst Differentiation</title><source>MEDLINE</source><source>JSTOR Archive Collection A-Z Listing</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Zhao, Yinhong ; Shi, Yunming ; Zhao, Weixing ; Huang, Xu ; Wang, Donghui ; Brown, Neil ; Brand, Jerry ; Zhao, Jindong ; Haselkorn, Robert</creator><creatorcontrib>Zhao, Yinhong ; Shi, Yunming ; Zhao, Weixing ; Huang, Xu ; Wang, Donghui ; Brown, Neil ; Brand, Jerry ; Zhao, Jindong ; Haselkorn, Robert</creatorcontrib><description>Although it is known that calcium is a very important messenger involved in many eukaryotic cellular processes, much less is known about calcium's role in bacteria. CcbP, a Ca2+-binding protein, was isolated from the heterocystous cyanobacterium Anabaena sp. PCC 7120, and the ccbP gene was cloned and inactivated. In the absence of combined nitrogen, inactivation of ccbP resulted in multiple contiguous heterocysts, whereas overexpression of ccbP suppressed heterocyst formation. Calmodulin, which is not present in Anabaena species, could also suppress heterocyst formation in both Anabaena sp. PCC 7120 and Anabaena variabilis. HetR induction upon nitrogen step-down was slow in the strain overexpressing ccbP. The Ca2+reporter protein obelin was used to show that mature heterocysts had a high intracellular free Ca2+concentration {[ Ca2+]i}, and immunoblotting showed that CcbP was absent from heterocysts. A regular pattern of cells with higher [ Ca2+]iwas established during heterocyst differentiation before the appearance of proheterocysts. A rapid increase of [ Ca2+]icould be detected 4 h after the removal of combined nitrogen, and this increase was suppressed by excessive CcbP. These results suggest that Ca2+ions play very important roles in hetR induction and heterocyst differentiation.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0501782102</identifier><identifier>PMID: 15811937</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Anabaena ; Anabaena - cytology ; Anabaena - physiology ; Anabaena variabilis ; Bacteria ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biological Sciences ; Calcium ; Calcium - metabolism ; Calcium-Binding Proteins - genetics ; Calcium-Binding Proteins - metabolism ; Calmodulin - metabolism ; Cyanobacterium ; Emission spectra ; Fluorescence ; Gene expression ; Gene Expression Regulation ; Gene Silencing ; Genes, Reporter ; Immunoblotting ; Ions ; Luminescent Proteins - metabolism ; Molecular Sequence Data ; Nitrogen ; Nitrogen - metabolism ; Plasmids ; Proteins ; Somatic cells</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2005-04, Vol.102 (16), p.5744-5748</ispartof><rights>Copyright 1993/2005 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Apr 19, 2005</rights><rights>Copyright © 2005, The National Academy of Sciences 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-b4a17b73ebad1e1fcc6c39315f41f4975ce8b6c56eabc72083e331fba0eb13eb3</citedby><cites>FETCH-LOGICAL-c526t-b4a17b73ebad1e1fcc6c39315f41f4975ce8b6c56eabc72083e331fba0eb13eb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/102/16.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3375378$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3375378$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15811937$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhao, Yinhong</creatorcontrib><creatorcontrib>Shi, Yunming</creatorcontrib><creatorcontrib>Zhao, Weixing</creatorcontrib><creatorcontrib>Huang, Xu</creatorcontrib><creatorcontrib>Wang, Donghui</creatorcontrib><creatorcontrib>Brown, Neil</creatorcontrib><creatorcontrib>Brand, Jerry</creatorcontrib><creatorcontrib>Zhao, Jindong</creatorcontrib><creatorcontrib>Haselkorn, Robert</creatorcontrib><title>CcbP, a Calcium-Binding Protein from Anabaena sp. PCC 7120, Provides Evidence That Calcium Ions Regulate Heterocyst Differentiation</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Although it is known that calcium is a very important messenger involved in many eukaryotic cellular processes, much less is known about calcium's role in bacteria. CcbP, a Ca2+-binding protein, was isolated from the heterocystous cyanobacterium Anabaena sp. PCC 7120, and the ccbP gene was cloned and inactivated. In the absence of combined nitrogen, inactivation of ccbP resulted in multiple contiguous heterocysts, whereas overexpression of ccbP suppressed heterocyst formation. Calmodulin, which is not present in Anabaena species, could also suppress heterocyst formation in both Anabaena sp. PCC 7120 and Anabaena variabilis. HetR induction upon nitrogen step-down was slow in the strain overexpressing ccbP. The Ca2+reporter protein obelin was used to show that mature heterocysts had a high intracellular free Ca2+concentration {[ Ca2+]i}, and immunoblotting showed that CcbP was absent from heterocysts. A regular pattern of cells with higher [ Ca2+]iwas established during heterocyst differentiation before the appearance of proheterocysts. A rapid increase of [ Ca2+]icould be detected 4 h after the removal of combined nitrogen, and this increase was suppressed by excessive CcbP. These results suggest that Ca2+ions play very important roles in hetR induction and heterocyst differentiation.</description><subject>Anabaena</subject><subject>Anabaena - cytology</subject><subject>Anabaena - physiology</subject><subject>Anabaena variabilis</subject><subject>Bacteria</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological Sciences</subject><subject>Calcium</subject><subject>Calcium - metabolism</subject><subject>Calcium-Binding Proteins - genetics</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Calmodulin - metabolism</subject><subject>Cyanobacterium</subject><subject>Emission spectra</subject><subject>Fluorescence</subject><subject>Gene expression</subject><subject>Gene Expression Regulation</subject><subject>Gene Silencing</subject><subject>Genes, Reporter</subject><subject>Immunoblotting</subject><subject>Ions</subject><subject>Luminescent Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Nitrogen</subject><subject>Nitrogen - metabolism</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>Somatic cells</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0jFv1DAUB_AIgehRmFkQWAyIobn6xXGcDAwlFFqpEidUZsvxvVx9ytmH7VR05ovj6I4eMMD0Bv_-T8_2y7LnQOdABTvdWhXmlFMQdQG0eJDNgDaQV2VDH2YzSguR12VRHmVPQlhTShte08fZEfAaoGFilv1odbc4IYq0atBm3OTvjV0auyIL7yIaS3rvNuTMqk6hVSRs52TRtkRAQU8mc2uWGMj5VKxGcn2j4q9W5NLZQL7gahxURHKBEb3TdyGSD6bv0aONRkXj7NPsUa-GgM_29Tj7-vH8ur3Irz5_umzPrnLNiyrmXalAdIJhp5aA0GtdadYw4H0JfdkIrrHuKs0rVJ0WBa0ZMgZ9pyh2kFLsOHu367sduw0udRrAq0FuvdkofyedMvLPE2tu5MrdSs4rBizl3-zz3n0bMUS5MUHjMCiLbgyyEoILaKr_QhCcVQ2rE3z9F1y70dv0CLKgUEINNU_odIe0dyF47O8nBiqnLZDTFsjDFqTEy98vevD7b0_g1R5MyUO7QkIluSjLJN7-W8h-HIaI32OiL3Z0HaLz95axdEtRs5-addAc</recordid><startdate>20050419</startdate><enddate>20050419</enddate><creator>Zhao, Yinhong</creator><creator>Shi, Yunming</creator><creator>Zhao, Weixing</creator><creator>Huang, Xu</creator><creator>Wang, Donghui</creator><creator>Brown, Neil</creator><creator>Brand, Jerry</creator><creator>Zhao, Jindong</creator><creator>Haselkorn, Robert</creator><general>National Academy of Sciences</general><general>National Acad Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20050419</creationdate><title>CcbP, a Calcium-Binding Protein from Anabaena sp. 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PCC 7120, Provides Evidence That Calcium Ions Regulate Heterocyst Differentiation</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2005-04-19</date><risdate>2005</risdate><volume>102</volume><issue>16</issue><spage>5744</spage><epage>5748</epage><pages>5744-5748</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Although it is known that calcium is a very important messenger involved in many eukaryotic cellular processes, much less is known about calcium's role in bacteria. CcbP, a Ca2+-binding protein, was isolated from the heterocystous cyanobacterium Anabaena sp. PCC 7120, and the ccbP gene was cloned and inactivated. In the absence of combined nitrogen, inactivation of ccbP resulted in multiple contiguous heterocysts, whereas overexpression of ccbP suppressed heterocyst formation. Calmodulin, which is not present in Anabaena species, could also suppress heterocyst formation in both Anabaena sp. PCC 7120 and Anabaena variabilis. HetR induction upon nitrogen step-down was slow in the strain overexpressing ccbP. The Ca2+reporter protein obelin was used to show that mature heterocysts had a high intracellular free Ca2+concentration {[ Ca2+]i}, and immunoblotting showed that CcbP was absent from heterocysts. A regular pattern of cells with higher [ Ca2+]iwas established during heterocyst differentiation before the appearance of proheterocysts. A rapid increase of [ Ca2+]icould be detected 4 h after the removal of combined nitrogen, and this increase was suppressed by excessive CcbP. These results suggest that Ca2+ions play very important roles in hetR induction and heterocyst differentiation.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>15811937</pmid><doi>10.1073/pnas.0501782102</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Anabaena Anabaena - cytology Anabaena - physiology Anabaena variabilis Bacteria Bacterial Proteins - genetics Bacterial Proteins - metabolism Biological Sciences Calcium Calcium - metabolism Calcium-Binding Proteins - genetics Calcium-Binding Proteins - metabolism Calmodulin - metabolism Cyanobacterium Emission spectra Fluorescence Gene expression Gene Expression Regulation Gene Silencing Genes, Reporter Immunoblotting Ions Luminescent Proteins - metabolism Molecular Sequence Data Nitrogen Nitrogen - metabolism Plasmids Proteins Somatic cells |
| title | CcbP, a Calcium-Binding Protein from Anabaena sp. PCC 7120, Provides Evidence That Calcium Ions Regulate Heterocyst Differentiation |
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