A novel twist on molecular interactions between thioredoxin and nicotinamide adenine dinucleotide phosphate-dependent thioredoxin reductase
The ubiquitous disulfide reductase thioredoxin (Trx) regulates several important biological processes such as seed germination in plants. Oxidized cytosolic Trx is regenerated by nicotinamide adenine dinucleotide phosphate (NADPH)‐dependent thioredoxin reductase (NTR) in a multistep transfer of redu...
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| Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2014-04, Vol.82 (4), p.607-619 |
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| container_title | Proteins, structure, function, and bioinformatics |
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| creator | Kirkensgaard, Kristine G. Hägglund, Per Shahpiri, Azar Finnie, Christine Henriksen, Anette Svensson, Birte |
| description | The ubiquitous disulfide reductase thioredoxin (Trx) regulates several important biological processes such as seed germination in plants. Oxidized cytosolic Trx is regenerated by nicotinamide adenine dinucleotide phosphate (NADPH)‐dependent thioredoxin reductase (NTR) in a multistep transfer of reducing equivalents from NADPH to Trx via a tightly NTR‐bound flavin. Here, interactions between NTR and Trx are predicted by molecular modelling of the barley NTR:Trx complex (HvNTR2:HvTrxh2) and probed by site directed mutagenesis. Enzyme kinetics analysis reveals mutants in a loop of the flavin adenine dinucleotide (FAD)‐binding domain of HvNTR2 to strongly affect the interaction with Trx. In particular, Trp42 and Met43 play key roles for recognition of the endogenous HvTrxh2. Trx from Arabidopsis thaliana is also efficiently recycled by HvNTR2 but turnover in this case appears to be less dependent on these two residues, suggesting a distinct mode for NTR:Trx recognition. Comparison between the HvNTR2:HvTrxh2 model and the crystal structure of the Escherichia coli NTR:Trx complex reveals major differences in interactions involving the FAD‐ and NADPH‐binding domains as supported by our experiments. Overall, the findings suggest that NTR:Trx interactions in different biological systems are fine‐tuned by multiple intermolecular contacts. Proteins 2014; 82:607–619. © 2013 Wiley Periodicals, Inc. |
| doi_str_mv | 10.1002/prot.24437 |
| format | Article |
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Oxidized cytosolic Trx is regenerated by nicotinamide adenine dinucleotide phosphate (NADPH)‐dependent thioredoxin reductase (NTR) in a multistep transfer of reducing equivalents from NADPH to Trx via a tightly NTR‐bound flavin. Here, interactions between NTR and Trx are predicted by molecular modelling of the barley NTR:Trx complex (HvNTR2:HvTrxh2) and probed by site directed mutagenesis. Enzyme kinetics analysis reveals mutants in a loop of the flavin adenine dinucleotide (FAD)‐binding domain of HvNTR2 to strongly affect the interaction with Trx. In particular, Trp42 and Met43 play key roles for recognition of the endogenous HvTrxh2. Trx from Arabidopsis thaliana is also efficiently recycled by HvNTR2 but turnover in this case appears to be less dependent on these two residues, suggesting a distinct mode for NTR:Trx recognition. Comparison between the HvNTR2:HvTrxh2 model and the crystal structure of the Escherichia coli NTR:Trx complex reveals major differences in interactions involving the FAD‐ and NADPH‐binding domains as supported by our experiments. Overall, the findings suggest that NTR:Trx interactions in different biological systems are fine‐tuned by multiple intermolecular contacts. 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Oxidized cytosolic Trx is regenerated by nicotinamide adenine dinucleotide phosphate (NADPH)‐dependent thioredoxin reductase (NTR) in a multistep transfer of reducing equivalents from NADPH to Trx via a tightly NTR‐bound flavin. Here, interactions between NTR and Trx are predicted by molecular modelling of the barley NTR:Trx complex (HvNTR2:HvTrxh2) and probed by site directed mutagenesis. Enzyme kinetics analysis reveals mutants in a loop of the flavin adenine dinucleotide (FAD)‐binding domain of HvNTR2 to strongly affect the interaction with Trx. In particular, Trp42 and Met43 play key roles for recognition of the endogenous HvTrxh2. Trx from Arabidopsis thaliana is also efficiently recycled by HvNTR2 but turnover in this case appears to be less dependent on these two residues, suggesting a distinct mode for NTR:Trx recognition. Comparison between the HvNTR2:HvTrxh2 model and the crystal structure of the Escherichia coli NTR:Trx complex reveals major differences in interactions involving the FAD‐ and NADPH‐binding domains as supported by our experiments. Overall, the findings suggest that NTR:Trx interactions in different biological systems are fine‐tuned by multiple intermolecular contacts. Proteins 2014; 82:607–619. © 2013 Wiley Periodicals, Inc.</description><subject>Amino Acid Sequence</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis thaliana</subject><subject>disulfide reduction</subject><subject>enzyme kinetics</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>homology modeling</subject><subject>Hordeum - enzymology</subject><subject>Hordeum vulgare</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>NADP - chemistry</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>protein-protein interactions</subject><subject>redox proteins</subject><subject>Sequence Alignment</subject><subject>site-directed mutagenesis</subject><subject>Thioredoxin-Disulfide Reductase - chemistry</subject><subject>Thioredoxins - chemistry</subject><issn>0887-3585</issn><issn>1097-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kV1LHDEUhkNpqavtjT9AAr0pwth8zCSTS7tUW5AqsuBlyGbOsrEzyTTJdPU3-KfNuiq0F716Iec5D4e8CB1SckIJYV_GGPIJq2su36AZJUpWhPL6LZqRtpUVb9pmD-2ndEsIEYqL92iP1ZRxRtUMPZxiH_5Aj_PGpYyDx0PowU69idj5DNHY7IJPeAl5A-BxXrsQoQt3zmPjO-ydDdl5M7gOsOnAOw-4c36yPZRBeRzXIY1rk6HqYARfkPyXpeRks0nwAb1bmT7Bx-c8QIuzb4v59-ri8vzH_PSisrWqZcUoJwKkZYKt5JKKElwJztiqVgQ6RZnhDRDOQNG24bCkrDVWWmFVIwThB-jzTlv-7fcEKevBJQt9bzyEKWnaMMJbKSkv6Kd_0NswRV-OKxSpOSWy2VLHO8rGkFKElR6jG0y815TobUN625B-aqjAR8_KaTlA94q-VFIAugM2rof7_6j01fXl4kVa7XZKh3D3umPiLy0kl42--Xmub9TXxXxeFC1_BM1QrNg</recordid><startdate>201404</startdate><enddate>201404</enddate><creator>Kirkensgaard, Kristine G.</creator><creator>Hägglund, Per</creator><creator>Shahpiri, Azar</creator><creator>Finnie, Christine</creator><creator>Henriksen, Anette</creator><creator>Svensson, Birte</creator><general>Blackwell Publishing Ltd</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</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>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>201404</creationdate><title>A novel twist on molecular interactions between thioredoxin and nicotinamide adenine dinucleotide phosphate-dependent thioredoxin reductase</title><author>Kirkensgaard, Kristine G. ; Hägglund, Per ; Shahpiri, Azar ; Finnie, Christine ; Henriksen, Anette ; Svensson, Birte</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4947-21306e7c262f7b1662f396322f490ed912a35e032e91853eb128ac7c6c956603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis thaliana</topic><topic>disulfide reduction</topic><topic>enzyme kinetics</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>homology modeling</topic><topic>Hordeum - enzymology</topic><topic>Hordeum vulgare</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>NADP - chemistry</topic><topic>Protein Conformation</topic><topic>Protein Structure, Tertiary</topic><topic>protein-protein interactions</topic><topic>redox proteins</topic><topic>Sequence Alignment</topic><topic>site-directed mutagenesis</topic><topic>Thioredoxin-Disulfide Reductase - chemistry</topic><topic>Thioredoxins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kirkensgaard, Kristine G.</creatorcontrib><creatorcontrib>Hägglund, Per</creatorcontrib><creatorcontrib>Shahpiri, Azar</creatorcontrib><creatorcontrib>Finnie, Christine</creatorcontrib><creatorcontrib>Henriksen, Anette</creatorcontrib><creatorcontrib>Svensson, Birte</creatorcontrib><collection>Istex</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>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</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>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Proteins, structure, function, and bioinformatics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kirkensgaard, Kristine G.</au><au>Hägglund, Per</au><au>Shahpiri, Azar</au><au>Finnie, Christine</au><au>Henriksen, Anette</au><au>Svensson, Birte</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel twist on molecular interactions between thioredoxin and nicotinamide adenine dinucleotide phosphate-dependent thioredoxin reductase</atitle><jtitle>Proteins, structure, function, and bioinformatics</jtitle><addtitle>Proteins</addtitle><date>2014-04</date><risdate>2014</risdate><volume>82</volume><issue>4</issue><spage>607</spage><epage>619</epage><pages>607-619</pages><issn>0887-3585</issn><eissn>1097-0134</eissn><abstract>The ubiquitous disulfide reductase thioredoxin (Trx) regulates several important biological processes such as seed germination in plants. Oxidized cytosolic Trx is regenerated by nicotinamide adenine dinucleotide phosphate (NADPH)‐dependent thioredoxin reductase (NTR) in a multistep transfer of reducing equivalents from NADPH to Trx via a tightly NTR‐bound flavin. Here, interactions between NTR and Trx are predicted by molecular modelling of the barley NTR:Trx complex (HvNTR2:HvTrxh2) and probed by site directed mutagenesis. Enzyme kinetics analysis reveals mutants in a loop of the flavin adenine dinucleotide (FAD)‐binding domain of HvNTR2 to strongly affect the interaction with Trx. In particular, Trp42 and Met43 play key roles for recognition of the endogenous HvTrxh2. Trx from Arabidopsis thaliana is also efficiently recycled by HvNTR2 but turnover in this case appears to be less dependent on these two residues, suggesting a distinct mode for NTR:Trx recognition. Comparison between the HvNTR2:HvTrxh2 model and the crystal structure of the Escherichia coli NTR:Trx complex reveals major differences in interactions involving the FAD‐ and NADPH‐binding domains as supported by our experiments. Overall, the findings suggest that NTR:Trx interactions in different biological systems are fine‐tuned by multiple intermolecular contacts. Proteins 2014; 82:607–619. © 2013 Wiley Periodicals, Inc.</abstract><cop>United States</cop><pub>Blackwell Publishing Ltd</pub><pmid>24123219</pmid><doi>10.1002/prot.24437</doi><tpages>13</tpages></addata></record> |
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| ispartof | Proteins, structure, function, and bioinformatics, 2014-04, Vol.82 (4), p.607-619 |
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| subjects | Amino Acid Sequence Arabidopsis - enzymology Arabidopsis thaliana disulfide reduction enzyme kinetics Escherichia coli Escherichia coli - enzymology homology modeling Hordeum - enzymology Hordeum vulgare Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed NADP - chemistry Protein Conformation Protein Structure, Tertiary protein-protein interactions redox proteins Sequence Alignment site-directed mutagenesis Thioredoxin-Disulfide Reductase - chemistry Thioredoxins - chemistry |
| title | A novel twist on molecular interactions between thioredoxin and nicotinamide adenine dinucleotide phosphate-dependent thioredoxin reductase |
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