Human serum albumin as a catalyst of RNA cleavage: N-Homocysteinylation and N-phosphorylation by oligonucleotide affinity reagent alter the reactivity of the protein
Kinetic parameters for the cleavage of UpA site in an oligonucleotide in the presence of human serum albumin (HSA) or one of its clinically relevant modification were measured. The RNA-hydrolyzing activity of HSA was decreased by its nonenzymatic N-homocysteinylation. According to 31P NMR data, Lys...
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| Veröffentlicht in: | Bioorganic & medicinal chemistry 2008-10, Vol.18 (20), p.5396-5398 |
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| container_title | Bioorganic & medicinal chemistry |
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| creator | Gerasimova, Yuliya V. Knorre, Dmitry D. Shakirov, Makhmut M. Godovikova, Tatyana S. |
| description | Kinetic parameters for the cleavage of UpA site in an oligonucleotide in the presence of human serum albumin (HSA) or one of its clinically relevant modification were measured. The RNA-hydrolyzing activity of HSA was decreased by its nonenzymatic N-homocysteinylation. According to
31P NMR data, Lys and Tyr residues were the labeling targets when a phosphorylating analog of oligoribonucleotide substrate was employed. The site of tyrosine modification was slowly dephosphorylated. Lys-directed affinity labeling suppressed oligonucleotide cleavage indicating that lysines took part in the reaction. |
| doi_str_mv | 10.1016/j.bmcl.2008.09.049 |
| format | Article |
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31P NMR data, Lys and Tyr residues were the labeling targets when a phosphorylating analog of oligoribonucleotide substrate was employed. The site of tyrosine modification was slowly dephosphorylated. Lys-directed affinity labeling suppressed oligonucleotide cleavage indicating that lysines took part in the reaction.</description><subject>Affinity labeling</subject><subject>Albumin</subject><subject>Catalysis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Homocysteine - chemistry</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Kinetics</subject><subject>Lysine - chemistry</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Chemical</subject><subject>Models, Statistical</subject><subject>N-Homocysteinylation</subject><subject>Oligonucleotides - chemistry</subject><subject>Phosphorylation</subject><subject>RNA - chemistry</subject><subject>RNA-hydrolyzing activity</subject><subject>Serum Albumin - chemistry</subject><subject>Tyrosine - chemistry</subject><issn>0960-894X</issn><issn>0968-0896</issn><issn>1464-3405</issn><issn>1464-3391</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2KFDEUhQtRnHb0BVxINs6u2qSSSqXEzTCoLQwjiIK7kJ-bmTRVlTZJNdQD-Z6m6FZ3ugiBe75zT8ipqpcEbwkm_M1-q0czbBuMxRb3W8z6R9WGMM5qynD7uNrgnuNa9Oz7RfUspT3GhGHGnlYXRIimp4Ruqp-7eVQTShDnEalBz6OfkEpIIaOyGpaUUXDoy901MgOoo7qHt-iu3oUxmKKBn5ZBZR-KZ7JFODyEVE78PdULCoO_D9Nc7CF7C0g55yefFxShbJtySc0QUX6AdWKyP65iCV0nhxjWkOfVE6eGBC_O92X17cP7rze7-vbzx08317e1YaTNteucbRkVWlNlWdu0orOtaIVqNaECLBTM8a5RlArqGGus0xpaqpy22ilHL6ur096S-2OGlOXok4FhUBOEOUne8452bfdfkPRccE55AZsTaGJIKYKTh-hHFRdJsFxblHu5tijXFiXuZWmxmF6dt896BPvXcq6tAK_PgEpGDS6qyfj0h2tw1wvcrdy7Ewfl044eokzGw2TA-ggmSxv8v97xC5Vzv8I</recordid><startdate>20081015</startdate><enddate>20081015</enddate><creator>Gerasimova, Yuliya V.</creator><creator>Knorre, Dmitry D.</creator><creator>Shakirov, Makhmut M.</creator><creator>Godovikova, Tatyana S.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</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>7QO</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20081015</creationdate><title>Human serum albumin as a catalyst of RNA cleavage: N-Homocysteinylation and N-phosphorylation by oligonucleotide affinity reagent alter the reactivity of the protein</title><author>Gerasimova, Yuliya V. ; Knorre, Dmitry D. ; Shakirov, Makhmut M. ; Godovikova, Tatyana S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-f7fd5438bb3ad452587d5858a5b138edec41f672a3383f442dfbbe53afbdbfaf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Affinity labeling</topic><topic>Albumin</topic><topic>Catalysis</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Homocysteine - chemistry</topic><topic>Humans</topic><topic>Hydrolysis</topic><topic>Kinetics</topic><topic>Lysine - chemistry</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Chemical</topic><topic>Models, Statistical</topic><topic>N-Homocysteinylation</topic><topic>Oligonucleotides - chemistry</topic><topic>Phosphorylation</topic><topic>RNA - chemistry</topic><topic>RNA-hydrolyzing activity</topic><topic>Serum Albumin - chemistry</topic><topic>Tyrosine - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gerasimova, Yuliya V.</creatorcontrib><creatorcontrib>Knorre, Dmitry D.</creatorcontrib><creatorcontrib>Shakirov, Makhmut M.</creatorcontrib><creatorcontrib>Godovikova, Tatyana S.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Bioorganic & medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gerasimova, Yuliya V.</au><au>Knorre, Dmitry D.</au><au>Shakirov, Makhmut M.</au><au>Godovikova, Tatyana S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human serum albumin as a catalyst of RNA cleavage: N-Homocysteinylation and N-phosphorylation by oligonucleotide affinity reagent alter the reactivity of the protein</atitle><jtitle>Bioorganic & medicinal chemistry</jtitle><addtitle>Bioorg Med Chem Lett</addtitle><date>2008-10-15</date><risdate>2008</risdate><volume>18</volume><issue>20</issue><spage>5396</spage><epage>5398</epage><pages>5396-5398</pages><issn>0960-894X</issn><issn>0968-0896</issn><eissn>1464-3405</eissn><eissn>1464-3391</eissn><abstract>Kinetic parameters for the cleavage of UpA site in an oligonucleotide in the presence of human serum albumin (HSA) or one of its clinically relevant modification were measured. The RNA-hydrolyzing activity of HSA was decreased by its nonenzymatic N-homocysteinylation. According to
31P NMR data, Lys and Tyr residues were the labeling targets when a phosphorylating analog of oligoribonucleotide substrate was employed. The site of tyrosine modification was slowly dephosphorylated. Lys-directed affinity labeling suppressed oligonucleotide cleavage indicating that lysines took part in the reaction.</abstract><cop>Amsterdam</cop><pub>Elsevier Ltd</pub><pmid>18829313</pmid><doi>10.1016/j.bmcl.2008.09.049</doi><tpages>3</tpages></addata></record> |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE |
| subjects | Affinity labeling Albumin Catalysis Electrophoresis, Polyacrylamide Gel Homocysteine - chemistry Humans Hydrolysis Kinetics Lysine - chemistry Magnetic Resonance Spectroscopy Models, Chemical Models, Statistical N-Homocysteinylation Oligonucleotides - chemistry Phosphorylation RNA - chemistry RNA-hydrolyzing activity Serum Albumin - chemistry Tyrosine - chemistry |
| title | Human serum albumin as a catalyst of RNA cleavage: N-Homocysteinylation and N-phosphorylation by oligonucleotide affinity reagent alter the reactivity of the protein |
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