Polyphosphate, cyclic AMP, guanosine tetraphosphate, and c-di-GMP reduce in vitro Lon activity
Lon protease is conserved from bacteria to humans and regulates cellular processes by degrading different classes of proteins including antitoxins, transcriptional activators, unfolded proteins, and free ribosomal proteins. Since we found that Lon has several putative cyclic diguanylate (c-di-GMP) b...
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| Veröffentlicht in: | Bioengineered 2014-07, Vol.5 (4), p.264-268 |
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| creator | Osbourne, Devon O Soo, Valerie WC Konieczny, Igor Wood, Thomas K |
| description | Lon protease is conserved from bacteria to humans and regulates cellular processes by degrading different classes of proteins including antitoxins, transcriptional activators, unfolded proteins, and free ribosomal proteins. Since we found that Lon has several putative cyclic diguanylate (c-di-GMP) binding sites and since Lon binds polyphosphate (polyP) and lipid polysaccharide, we hypothesized that Lon has an affinity for phosphate-based molecules that might regulate its activity. Hence we tested the effect of polyP, cyclic adenosine monophosphate (cAMP), cyclic guanosine monophosphate (cGMP), guanosine tetraphosphate (ppGpp), c-di-GMP, and GMP on the ability of Lon to degrade α-casein. Inhibition of in vitro Lon activity occurred for polyP, cAMP, ppGpp, and c-di-GMP. We also demonstrated by HPLC that Lon is able to bind c-di-GMP. Therefore, four cell signals were found to regulate the activity of Lon protease. |
| doi_str_mv | 10.4161/bioe.29261 |
| format | Article |
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Since we found that Lon has several putative cyclic diguanylate (c-di-GMP) binding sites and since Lon binds polyphosphate (polyP) and lipid polysaccharide, we hypothesized that Lon has an affinity for phosphate-based molecules that might regulate its activity. Hence we tested the effect of polyP, cyclic adenosine monophosphate (cAMP), cyclic guanosine monophosphate (cGMP), guanosine tetraphosphate (ppGpp), c-di-GMP, and GMP on the ability of Lon to degrade α-casein. Inhibition of in vitro Lon activity occurred for polyP, cAMP, ppGpp, and c-di-GMP. We also demonstrated by HPLC that Lon is able to bind c-di-GMP. 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Therefore, four cell signals were found to regulate the activity of Lon protease.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>c-di-GMP</subject><subject>cAMP</subject><subject>Caseins - chemistry</subject><subject>Cyclic AMP - chemistry</subject><subject>Cyclic GMP - analogs & derivatives</subject><subject>Cyclic GMP - chemistry</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Guanosine Tetraphosphate - chemistry</subject><subject>Lon protease</subject><subject>Molecular Sequence Data</subject><subject>polyphosphate</subject><subject>Polyphosphates - chemistry</subject><subject>ppGpp</subject><subject>Protease La - chemistry</subject><subject>Proteolysis</subject><subject>Research Paper</subject><issn>2165-5979</issn><issn>2165-5987</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkVFrFDEQx4MottS--AEkjyLdmtkkm82LUIpthSveg74astlJL7KXnMluy357t149Kvg0M8yP_wz8CHkL7FxAAx-7kPC81nUDL8hxDY2spG7Vy0Ov9BE5LeUnYwwYF1K1r8lRLVolWsaOyY91GubdJpXdxo54Rt3shuDoxe36jN5NNqYSItIRx2yfUTb21FV9qK5v1zRjPzmkIdL7MOZEVylS68awTPMb8srboeDpUz0h368-f7u8qVZfr79cXqwqJ7QYK9SAqleCO9co7SXUfS-558KC9A34rtbImGy4EqxlHFpuO89ci-BakLrjJ-TTPnc3dVvsHcbl4cHsctjaPJtkg_l3E8PG3KV7I0BwrtUS8P4pIKdfE5bRbENxOAw2YpqKASm5gho4LOiHPepyKiWjP5wBZh6dmEcn5o-TBX73_LED-tfAAsg9EKJPeWsfUh56M9p5SNlnG10ohv8n-DfAfZpR</recordid><startdate>20140701</startdate><enddate>20140701</enddate><creator>Osbourne, Devon O</creator><creator>Soo, Valerie WC</creator><creator>Konieczny, Igor</creator><creator>Wood, Thomas K</creator><general>Taylor & Francis</general><general>Landes Bioscience</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20140701</creationdate><title>Polyphosphate, cyclic AMP, guanosine tetraphosphate, and c-di-GMP reduce in vitro Lon activity</title><author>Osbourne, Devon O ; Soo, Valerie WC ; Konieczny, Igor ; Wood, Thomas K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c494t-e91e7d743cc679f512dd53f34a15f61fb29e00563740803183abf0c8e1c8159b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>c-di-GMP</topic><topic>cAMP</topic><topic>Caseins - chemistry</topic><topic>Cyclic AMP - chemistry</topic><topic>Cyclic GMP - analogs & derivatives</topic><topic>Cyclic GMP - chemistry</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Guanosine Tetraphosphate - chemistry</topic><topic>Lon protease</topic><topic>Molecular Sequence Data</topic><topic>polyphosphate</topic><topic>Polyphosphates - chemistry</topic><topic>ppGpp</topic><topic>Protease La - chemistry</topic><topic>Proteolysis</topic><topic>Research Paper</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Osbourne, Devon O</creatorcontrib><creatorcontrib>Soo, Valerie WC</creatorcontrib><creatorcontrib>Konieczny, Igor</creatorcontrib><creatorcontrib>Wood, Thomas K</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Bioengineered</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Osbourne, Devon O</au><au>Soo, Valerie WC</au><au>Konieczny, Igor</au><au>Wood, Thomas K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Polyphosphate, cyclic AMP, guanosine tetraphosphate, and c-di-GMP reduce in vitro Lon activity</atitle><jtitle>Bioengineered</jtitle><addtitle>Bioengineered</addtitle><date>2014-07-01</date><risdate>2014</risdate><volume>5</volume><issue>4</issue><spage>264</spage><epage>268</epage><pages>264-268</pages><issn>2165-5979</issn><eissn>2165-5987</eissn><abstract>Lon protease is conserved from bacteria to humans and regulates cellular processes by degrading different classes of proteins including antitoxins, transcriptional activators, unfolded proteins, and free ribosomal proteins. 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| subjects | Amino Acid Sequence Binding Sites c-di-GMP cAMP Caseins - chemistry Cyclic AMP - chemistry Cyclic GMP - analogs & derivatives Cyclic GMP - chemistry Escherichia coli - enzymology Escherichia coli Proteins - chemistry Guanosine Tetraphosphate - chemistry Lon protease Molecular Sequence Data polyphosphate Polyphosphates - chemistry ppGpp Protease La - chemistry Proteolysis Research Paper |
| title | Polyphosphate, cyclic AMP, guanosine tetraphosphate, and c-di-GMP reduce in vitro Lon activity |
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