Cyclic Di-AMP Impairs Potassium Uptake Mediated by a Cyclic Di-AMP Binding Protein in Streptococcus pneumoniae
Cyclic di-AMP (c-di-AMP) has been shown to play important roles as a second messenger in bacterial physiology and infections. However, understanding of how the signal is transduced is still limited. Previously, we have characterized a diadenylate cyclase and two c-di-AMP phosphodiesterases in Strept...
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| Veröffentlicht in: | Journal of Bacteriology 2014-02, Vol.196 (3), p.614-623 |
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| creator | Bai, Yinlan Yang, Jun Zarrella, Tiffany M Zhang, Yang Metzger, Dennis W Bai, Guangchun |
| description | Cyclic di-AMP (c-di-AMP) has been shown to play important roles as a second messenger in bacterial physiology and infections. However, understanding of how the signal is transduced is still limited. Previously, we have characterized a diadenylate cyclase and two c-di-AMP phosphodiesterases in Streptococcus pneumoniae, a Gram-positive pathogen. In this study, we identified a c-di-AMP binding protein (CabP) in S. pneumoniae using c-di-AMP affinity chromatography. We demonstrated that CabP specifically bound c-di-AMP and that this interaction could not be interrupted by competition with other nucleotides, including ATP, cAMP, AMP, phosphoadenylyl adenosine (pApA), and cyclic di-GMP (c-di-GMP). By using a bacterial two-hybrid system and genetic mutagenesis, we showed that CabP directly interacted with a potassium transporter (SPD_0076) and that both proteins were required for pneumococcal growth in media with low concentrations of potassium. Interestingly, the interaction between CabP and SPD_0076 and the efficiency of potassium uptake were impaired by elevated c-di-AMP in pneumococci. These results establish a direct c-di-AMP-mediated signaling pathway that regulates pneumococcal potassium uptake. |
| doi_str_mv | 10.1128/jb.01041-13 |
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However, understanding of how the signal is transduced is still limited. Previously, we have characterized a diadenylate cyclase and two c-di-AMP phosphodiesterases in Streptococcus pneumoniae, a Gram-positive pathogen. In this study, we identified a c-di-AMP binding protein (CabP) in S. pneumoniae using c-di-AMP affinity chromatography. We demonstrated that CabP specifically bound c-di-AMP and that this interaction could not be interrupted by competition with other nucleotides, including ATP, cAMP, AMP, phosphoadenylyl adenosine (pApA), and cyclic di-GMP (c-di-GMP). By using a bacterial two-hybrid system and genetic mutagenesis, we showed that CabP directly interacted with a potassium transporter (SPD_0076) and that both proteins were required for pneumococcal growth in media with low concentrations of potassium. Interestingly, the interaction between CabP and SPD_0076 and the efficiency of potassium uptake were impaired by elevated c-di-AMP in pneumococci. These results establish a direct c-di-AMP-mediated signaling pathway that regulates pneumococcal potassium uptake.</description><identifier>ISSN: 0021-9193</identifier><identifier>EISSN: 1098-5530</identifier><identifier>EISSN: 1067-8832</identifier><identifier>DOI: 10.1128/jb.01041-13</identifier><identifier>PMID: 24272783</identifier><identifier>CODEN: JOBAAY</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>adenosine ; adenosine monophosphate ; Adenosine triphosphatase ; adenosine triphosphate ; affinity chromatography ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacteriology ; binding proteins ; Biological Transport ; Chromatography ; culture media ; Dinucleoside Phosphates - genetics ; Dinucleoside Phosphates - metabolism ; Gene Expression Regulation, Bacterial ; Gram-positive bacteria ; microbial physiology ; Mutagenesis ; pathogens ; Potassium ; Potassium - metabolism ; signal transduction ; Streptococcus infections ; Streptococcus pneumoniae ; Streptococcus pneumoniae - genetics ; Streptococcus pneumoniae - metabolism ; two hybrid system techniques</subject><ispartof>Journal of Bacteriology, 2014-02, Vol.196 (3), p.614-623</ispartof><rights>Copyright American Society for Microbiology Feb 2014</rights><rights>Copyright © 2014, American Society for Microbiology. All Rights Reserved. 2014 American Society for Microbiology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c632t-868e07a6a9e605975f4428fe2890d7b1a44de0054642e454b80ebdd6660dacb3</citedby><cites>FETCH-LOGICAL-c632t-868e07a6a9e605975f4428fe2890d7b1a44de0054642e454b80ebdd6660dacb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3911161/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3911161/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24272783$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bai, Yinlan</creatorcontrib><creatorcontrib>Yang, Jun</creatorcontrib><creatorcontrib>Zarrella, Tiffany M</creatorcontrib><creatorcontrib>Zhang, Yang</creatorcontrib><creatorcontrib>Metzger, Dennis W</creatorcontrib><creatorcontrib>Bai, Guangchun</creatorcontrib><title>Cyclic Di-AMP Impairs Potassium Uptake Mediated by a Cyclic Di-AMP Binding Protein in Streptococcus pneumoniae</title><title>Journal of Bacteriology</title><addtitle>J Bacteriol</addtitle><description>Cyclic di-AMP (c-di-AMP) has been shown to play important roles as a second messenger in bacterial physiology and infections. However, understanding of how the signal is transduced is still limited. Previously, we have characterized a diadenylate cyclase and two c-di-AMP phosphodiesterases in Streptococcus pneumoniae, a Gram-positive pathogen. In this study, we identified a c-di-AMP binding protein (CabP) in S. pneumoniae using c-di-AMP affinity chromatography. We demonstrated that CabP specifically bound c-di-AMP and that this interaction could not be interrupted by competition with other nucleotides, including ATP, cAMP, AMP, phosphoadenylyl adenosine (pApA), and cyclic di-GMP (c-di-GMP). By using a bacterial two-hybrid system and genetic mutagenesis, we showed that CabP directly interacted with a potassium transporter (SPD_0076) and that both proteins were required for pneumococcal growth in media with low concentrations of potassium. Interestingly, the interaction between CabP and SPD_0076 and the efficiency of potassium uptake were impaired by elevated c-di-AMP in pneumococci. These results establish a direct c-di-AMP-mediated signaling pathway that regulates pneumococcal potassium uptake.</description><subject>adenosine</subject><subject>adenosine monophosphate</subject><subject>Adenosine triphosphatase</subject><subject>adenosine triphosphate</subject><subject>affinity chromatography</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>binding proteins</subject><subject>Biological Transport</subject><subject>Chromatography</subject><subject>culture media</subject><subject>Dinucleoside Phosphates - genetics</subject><subject>Dinucleoside Phosphates - metabolism</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Gram-positive bacteria</subject><subject>microbial physiology</subject><subject>Mutagenesis</subject><subject>pathogens</subject><subject>Potassium</subject><subject>Potassium - metabolism</subject><subject>signal transduction</subject><subject>Streptococcus infections</subject><subject>Streptococcus pneumoniae</subject><subject>Streptococcus pneumoniae - genetics</subject><subject>Streptococcus pneumoniae - metabolism</subject><subject>two hybrid system techniques</subject><issn>0021-9193</issn><issn>1098-5530</issn><issn>1067-8832</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0k1v1DAQBuAIgehSOHEHS1yQUMqM4zj2BaldvopasVLbs-Ukk10vSRzsBLT_nixbKsoFyZIPfjwa-50keY5wgsjV2215AggCU8weJAsErdI8z-BhsgDgmGrU2VHyJMYtAAqR88fJERe84IXKFkm_3FWtq9h7l55erth5N1gXIlv50cbopo7dDKP9RuySamdHqlm5Y5bdv3Tm-tr1a7YKfiTXs3ldjYGG0Ve-qqbIhp6mzvfO0tPkUWPbSM9u9-Pk-uOH6-Xn9OLrp_Pl6UVayYyPqZKKoLDSapKQ6yJvhOCqIa401EWJVoiaAHIhBSeRi1IBlXUtpYTaVmV2nLw7lB2msqO6on4MtjVDcJ0NO-OtM_dPercxa__DZBoRJc4FXt8WCP77RHE0nYsVta3tyU_RoCxUXiAU8H8qtFRaohYzffUP3fop9PNHzKpQgFJoPas3B1UFH2Og5q5vBLNP3Hw5M78TN5jN-sXfT72zfyKeATuAjVtvfrpAxsbObEuDWprMSNz39fJAGuuNXQcXzc0VB8z3E1PMQ5P9AgYZuN8</recordid><startdate>20140201</startdate><enddate>20140201</enddate><creator>Bai, Yinlan</creator><creator>Yang, Jun</creator><creator>Zarrella, Tiffany M</creator><creator>Zhang, Yang</creator><creator>Metzger, Dennis W</creator><creator>Bai, Guangchun</creator><general>American Society for Microbiology</general><scope>FBQ</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>7TM</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>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20140201</creationdate><title>Cyclic Di-AMP Impairs Potassium Uptake Mediated by a Cyclic Di-AMP Binding Protein in Streptococcus pneumoniae</title><author>Bai, Yinlan ; Yang, Jun ; Zarrella, Tiffany M ; Zhang, Yang ; Metzger, Dennis W ; Bai, Guangchun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c632t-868e07a6a9e605975f4428fe2890d7b1a44de0054642e454b80ebdd6660dacb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>adenosine</topic><topic>adenosine monophosphate</topic><topic>Adenosine triphosphatase</topic><topic>adenosine triphosphate</topic><topic>affinity chromatography</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>binding proteins</topic><topic>Biological Transport</topic><topic>Chromatography</topic><topic>culture media</topic><topic>Dinucleoside Phosphates - genetics</topic><topic>Dinucleoside Phosphates - metabolism</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Gram-positive bacteria</topic><topic>microbial physiology</topic><topic>Mutagenesis</topic><topic>pathogens</topic><topic>Potassium</topic><topic>Potassium - metabolism</topic><topic>signal transduction</topic><topic>Streptococcus infections</topic><topic>Streptococcus pneumoniae</topic><topic>Streptococcus pneumoniae - genetics</topic><topic>Streptococcus pneumoniae - metabolism</topic><topic>two hybrid system techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bai, Yinlan</creatorcontrib><creatorcontrib>Yang, Jun</creatorcontrib><creatorcontrib>Zarrella, Tiffany M</creatorcontrib><creatorcontrib>Zhang, Yang</creatorcontrib><creatorcontrib>Metzger, Dennis W</creatorcontrib><creatorcontrib>Bai, Guangchun</creatorcontrib><collection>AGRIS</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>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of Bacteriology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bai, Yinlan</au><au>Yang, Jun</au><au>Zarrella, Tiffany M</au><au>Zhang, Yang</au><au>Metzger, Dennis W</au><au>Bai, Guangchun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cyclic Di-AMP Impairs Potassium Uptake Mediated by a Cyclic Di-AMP Binding Protein in Streptococcus pneumoniae</atitle><jtitle>Journal of Bacteriology</jtitle><addtitle>J Bacteriol</addtitle><date>2014-02-01</date><risdate>2014</risdate><volume>196</volume><issue>3</issue><spage>614</spage><epage>623</epage><pages>614-623</pages><issn>0021-9193</issn><eissn>1098-5530</eissn><eissn>1067-8832</eissn><coden>JOBAAY</coden><abstract>Cyclic di-AMP (c-di-AMP) has been shown to play important roles as a second messenger in bacterial physiology and infections. However, understanding of how the signal is transduced is still limited. Previously, we have characterized a diadenylate cyclase and two c-di-AMP phosphodiesterases in Streptococcus pneumoniae, a Gram-positive pathogen. In this study, we identified a c-di-AMP binding protein (CabP) in S. pneumoniae using c-di-AMP affinity chromatography. We demonstrated that CabP specifically bound c-di-AMP and that this interaction could not be interrupted by competition with other nucleotides, including ATP, cAMP, AMP, phosphoadenylyl adenosine (pApA), and cyclic di-GMP (c-di-GMP). By using a bacterial two-hybrid system and genetic mutagenesis, we showed that CabP directly interacted with a potassium transporter (SPD_0076) and that both proteins were required for pneumococcal growth in media with low concentrations of potassium. Interestingly, the interaction between CabP and SPD_0076 and the efficiency of potassium uptake were impaired by elevated c-di-AMP in pneumococci. These results establish a direct c-di-AMP-mediated signaling pathway that regulates pneumococcal potassium uptake.</abstract><cop>United States</cop><pub>American Society for Microbiology</pub><pmid>24272783</pmid><doi>10.1128/jb.01041-13</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of Bacteriology, 2014-02, Vol.196 (3), p.614-623 |
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| language | eng |
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| subjects | adenosine adenosine monophosphate Adenosine triphosphatase adenosine triphosphate affinity chromatography Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology binding proteins Biological Transport Chromatography culture media Dinucleoside Phosphates - genetics Dinucleoside Phosphates - metabolism Gene Expression Regulation, Bacterial Gram-positive bacteria microbial physiology Mutagenesis pathogens Potassium Potassium - metabolism signal transduction Streptococcus infections Streptococcus pneumoniae Streptococcus pneumoniae - genetics Streptococcus pneumoniae - metabolism two hybrid system techniques |
| title | Cyclic Di-AMP Impairs Potassium Uptake Mediated by a Cyclic Di-AMP Binding Protein in Streptococcus pneumoniae |
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