Purification of a NAD(P) Reductase-Like Protein from the Thermogenic Appendix of the Sauromatum guttatum Inflorescence
A NAD(P) reductase-like protein with a molecular mass of 34.146 ± 34 Da was purified to homogeneity from the appendix of the inflorescence of the Sauromatum guttatum . On-line liquid chromatography/electrospray ionization-mass spectrometry was used to isolate and quantify the protein. For the identi...
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description | A NAD(P) reductase-like protein with a molecular mass of 34.146 ± 34 Da was purified to homogeneity from the appendix of the inflorescence of the
Sauromatum guttatum
. On-line liquid chromatography/electrospray ionization-mass spectrometry was used to isolate and quantify the protein. For the identification of the protein, liquid chromatography/electrospray ionization-tandem mass spectrometry analysis of tryptic digests of the protein was carried out. The acquired mass spectra were used for database searching, which led to the identification of a single tryptic peptide. The 12 amino acid tryptic peptide (FLPSEFGNDVDR) was found to be identical to amino acid residues at the positions 108–120 of isoflavone reductase in the
Arabidopsis
genome. A BLAST search identified this sequence region as unique and specific to a class of NAD(P)-dependent reductases involved in phenylpropanoid biosynthesis. Edman degradation revealed that the protein was N-terminally blocked. The amount of the protein (termed RL, NAD(P) reductase-like protein) increased 60-fold from D-4 (4 days before inflorescence-opening, designated as D-day) to D-Day, and declined the following day, when heat-production ceased. When salicylic acid, the endogenous trigger of heat-production in the
Sauromatum
appendix, was applied to premature appendices, a fivefold decrease in the amount of RL was detected in the treated section relative to the non-treated section. About 40 % of RL was found in the cytoplasm. Another 30 % was detected in Percoll-purified mitochondria and the rest, about 30 % was associated with a low speed centrifugation pellet due to nuclei and amyloplast localization. RL was also found in other thermogenic plants and detected in
Arabidopsis
leaves. The function of RL in thermogenic and non-thermogenic plants requires further investigation. |
doi_str_mv | 10.1007/s10930-013-9472-7 |
format | Article |
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Sauromatum guttatum
. On-line liquid chromatography/electrospray ionization-mass spectrometry was used to isolate and quantify the protein. For the identification of the protein, liquid chromatography/electrospray ionization-tandem mass spectrometry analysis of tryptic digests of the protein was carried out. The acquired mass spectra were used for database searching, which led to the identification of a single tryptic peptide. The 12 amino acid tryptic peptide (FLPSEFGNDVDR) was found to be identical to amino acid residues at the positions 108–120 of isoflavone reductase in the
Arabidopsis
genome. A BLAST search identified this sequence region as unique and specific to a class of NAD(P)-dependent reductases involved in phenylpropanoid biosynthesis. Edman degradation revealed that the protein was N-terminally blocked. The amount of the protein (termed RL, NAD(P) reductase-like protein) increased 60-fold from D-4 (4 days before inflorescence-opening, designated as D-day) to D-Day, and declined the following day, when heat-production ceased. When salicylic acid, the endogenous trigger of heat-production in the
Sauromatum
appendix, was applied to premature appendices, a fivefold decrease in the amount of RL was detected in the treated section relative to the non-treated section. About 40 % of RL was found in the cytoplasm. Another 30 % was detected in Percoll-purified mitochondria and the rest, about 30 % was associated with a low speed centrifugation pellet due to nuclei and amyloplast localization. RL was also found in other thermogenic plants and detected in
Arabidopsis
leaves. The function of RL in thermogenic and non-thermogenic plants requires further investigation.</description><identifier>ISSN: 1572-3887</identifier><identifier>EISSN: 1573-4943</identifier><identifier>EISSN: 1875-8355</identifier><identifier>DOI: 10.1007/s10930-013-9472-7</identifier><identifier>PMID: 23467808</identifier><language>eng</language><publisher>Boston: Springer US</publisher><subject>Amino acids ; Analysis ; Animal Anatomy ; Arabidopsis thaliana ; Araceae - enzymology ; Araceae - genetics ; Araceae - growth & development ; Araceae - metabolism ; Biochemistry ; Bioorganic Chemistry ; Biosynthesis ; Centrifugation ; Chemistry ; Chemistry and Materials Science ; Cytoplasm ; Database searching ; Ethylenediaminetetraacetic acid ; Flowers & plants ; Flowers - chemistry ; Flowers - enzymology ; Flowers - genetics ; Flowers - growth & development ; Genomics ; Histology ; Internet/Web search services ; Ionization ; Kinetics ; Liquid chromatography ; Mass spectra ; Mass spectrometry ; Molecular Weight ; Morphology ; NAD - metabolism ; Online searching ; Organic Chemistry ; Oxidoreductases - chemistry ; Oxidoreductases - genetics ; Oxidoreductases - isolation & purification ; Oxidoreductases - metabolism ; Plant biology ; Plant Components, Aerial - enzymology ; Plant Components, Aerial - genetics ; Plant Components, Aerial - metabolism ; Plant Proteins - chemistry ; Plant Proteins - genetics ; Plant Proteins - isolation & purification ; Plant Proteins - metabolism ; Povidone ; Protein Transport ; Proteins</subject><ispartof>The Protein Journal, 2013-03, Vol.32 (3), p.197-207</ispartof><rights>Springer Science+Business Media New York 2013</rights><rights>COPYRIGHT 2013 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-16873e7c0e62bf28e446cabcc949ac8e672c08a7aa365771b49591686c7f5e273</citedby><cites>FETCH-LOGICAL-c439t-16873e7c0e62bf28e446cabcc949ac8e672c08a7aa365771b49591686c7f5e273</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10930-013-9472-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10930-013-9472-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,781,785,27925,27926,41489,42558,51320</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23467808$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Skubatz, Hanna</creatorcontrib><creatorcontrib>Howald, William N.</creatorcontrib><title>Purification of a NAD(P) Reductase-Like Protein from the Thermogenic Appendix of the Sauromatum guttatum Inflorescence</title><title>The Protein Journal</title><addtitle>Protein J</addtitle><addtitle>Protein J</addtitle><description>A NAD(P) reductase-like protein with a molecular mass of 34.146 ± 34 Da was purified to homogeneity from the appendix of the inflorescence of the
Sauromatum guttatum
. On-line liquid chromatography/electrospray ionization-mass spectrometry was used to isolate and quantify the protein. For the identification of the protein, liquid chromatography/electrospray ionization-tandem mass spectrometry analysis of tryptic digests of the protein was carried out. The acquired mass spectra were used for database searching, which led to the identification of a single tryptic peptide. The 12 amino acid tryptic peptide (FLPSEFGNDVDR) was found to be identical to amino acid residues at the positions 108–120 of isoflavone reductase in the
Arabidopsis
genome. A BLAST search identified this sequence region as unique and specific to a class of NAD(P)-dependent reductases involved in phenylpropanoid biosynthesis. Edman degradation revealed that the protein was N-terminally blocked. The amount of the protein (termed RL, NAD(P) reductase-like protein) increased 60-fold from D-4 (4 days before inflorescence-opening, designated as D-day) to D-Day, and declined the following day, when heat-production ceased. When salicylic acid, the endogenous trigger of heat-production in the
Sauromatum
appendix, was applied to premature appendices, a fivefold decrease in the amount of RL was detected in the treated section relative to the non-treated section. About 40 % of RL was found in the cytoplasm. Another 30 % was detected in Percoll-purified mitochondria and the rest, about 30 % was associated with a low speed centrifugation pellet due to nuclei and amyloplast localization. RL was also found in other thermogenic plants and detected in
Arabidopsis
leaves. The function of RL in thermogenic and non-thermogenic plants requires further investigation.</description><subject>Amino acids</subject><subject>Analysis</subject><subject>Animal Anatomy</subject><subject>Arabidopsis thaliana</subject><subject>Araceae - enzymology</subject><subject>Araceae - genetics</subject><subject>Araceae - growth & development</subject><subject>Araceae - metabolism</subject><subject>Biochemistry</subject><subject>Bioorganic Chemistry</subject><subject>Biosynthesis</subject><subject>Centrifugation</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Cytoplasm</subject><subject>Database searching</subject><subject>Ethylenediaminetetraacetic acid</subject><subject>Flowers & plants</subject><subject>Flowers - chemistry</subject><subject>Flowers - enzymology</subject><subject>Flowers - genetics</subject><subject>Flowers - growth & development</subject><subject>Genomics</subject><subject>Histology</subject><subject>Internet/Web search services</subject><subject>Ionization</subject><subject>Kinetics</subject><subject>Liquid chromatography</subject><subject>Mass spectra</subject><subject>Mass spectrometry</subject><subject>Molecular Weight</subject><subject>Morphology</subject><subject>NAD - metabolism</subject><subject>Online searching</subject><subject>Organic Chemistry</subject><subject>Oxidoreductases - chemistry</subject><subject>Oxidoreductases - genetics</subject><subject>Oxidoreductases - isolation & purification</subject><subject>Oxidoreductases - metabolism</subject><subject>Plant biology</subject><subject>Plant Components, Aerial - enzymology</subject><subject>Plant Components, Aerial - genetics</subject><subject>Plant Components, Aerial - metabolism</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - isolation & purification</subject><subject>Plant Proteins - metabolism</subject><subject>Povidone</subject><subject>Protein Transport</subject><subject>Proteins</subject><issn>1572-3887</issn><issn>1573-4943</issn><issn>1875-8355</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kctuFDEQRVuIiITAB7BBltiERQe_2m4vR-EVaRRGENaWx1OeOHTbg-1G8Pe4M0l4COSFS1XnXlXpNs0zgk8JxvJVJlgx3GLCWsUlbeWD5oh0krVccfbwpqYt63t52DzO-Rpj2itJHzWHlHEhe9wfNd9WU_LOW1N8DCg6ZNDF4vXJ6iX6CJvJFpOhXfovgFYpFvABuRRHVK4AXV5BGuMWgrdosdtB2Pjvs8E8-2SmipkyjWg7lXJTnAc3xATZQrDwpDlwZsjw9PY_bj6_fXN59r5dfnh3frZYtpYzVVoieslAWgyCrh3tgXNhzdpaxZWxPQhJLe6NNIaJTkqy5qpTVSSsdB1QyY6bk73vLsWvE-SiR183GAYTIE5ZE0YJY12HcUVf_IVexymFut1MUa6YEOQXtTUDaB9cLMnY2VQvJBGzE6aVOv0HVd8GRm9jAOdr_w8B2QtsijkncHqX_GjSD02wnrPW-6x1zVrPWev5tue3C0_rETb3irtwK0D3QK6jsIX020X_df0JFr6x2g</recordid><startdate>20130301</startdate><enddate>20130301</enddate><creator>Skubatz, Hanna</creator><creator>Howald, William N.</creator><general>Springer US</general><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7TK</scope><scope>7TM</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20130301</creationdate><title>Purification of a NAD(P) Reductase-Like Protein from the Thermogenic Appendix of the Sauromatum guttatum Inflorescence</title><author>Skubatz, Hanna ; Howald, William N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-16873e7c0e62bf28e446cabcc949ac8e672c08a7aa365771b49591686c7f5e273</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino acids</topic><topic>Analysis</topic><topic>Animal Anatomy</topic><topic>Arabidopsis thaliana</topic><topic>Araceae - enzymology</topic><topic>Araceae - genetics</topic><topic>Araceae - growth & development</topic><topic>Araceae - metabolism</topic><topic>Biochemistry</topic><topic>Bioorganic Chemistry</topic><topic>Biosynthesis</topic><topic>Centrifugation</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Cytoplasm</topic><topic>Database searching</topic><topic>Ethylenediaminetetraacetic acid</topic><topic>Flowers & plants</topic><topic>Flowers - chemistry</topic><topic>Flowers - enzymology</topic><topic>Flowers - genetics</topic><topic>Flowers - growth & development</topic><topic>Genomics</topic><topic>Histology</topic><topic>Internet/Web search services</topic><topic>Ionization</topic><topic>Kinetics</topic><topic>Liquid chromatography</topic><topic>Mass spectra</topic><topic>Mass spectrometry</topic><topic>Molecular Weight</topic><topic>Morphology</topic><topic>NAD - metabolism</topic><topic>Online searching</topic><topic>Organic Chemistry</topic><topic>Oxidoreductases - chemistry</topic><topic>Oxidoreductases - genetics</topic><topic>Oxidoreductases - isolation & purification</topic><topic>Oxidoreductases - metabolism</topic><topic>Plant biology</topic><topic>Plant Components, Aerial - enzymology</topic><topic>Plant Components, Aerial - genetics</topic><topic>Plant Components, Aerial - metabolism</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - isolation & purification</topic><topic>Plant Proteins - metabolism</topic><topic>Povidone</topic><topic>Protein Transport</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Skubatz, Hanna</creatorcontrib><creatorcontrib>Howald, William N.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Protein Journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Skubatz, Hanna</au><au>Howald, William N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification of a NAD(P) Reductase-Like Protein from the Thermogenic Appendix of the Sauromatum guttatum Inflorescence</atitle><jtitle>The Protein Journal</jtitle><stitle>Protein J</stitle><addtitle>Protein J</addtitle><date>2013-03-01</date><risdate>2013</risdate><volume>32</volume><issue>3</issue><spage>197</spage><epage>207</epage><pages>197-207</pages><issn>1572-3887</issn><eissn>1573-4943</eissn><eissn>1875-8355</eissn><abstract>A NAD(P) reductase-like protein with a molecular mass of 34.146 ± 34 Da was purified to homogeneity from the appendix of the inflorescence of the
Sauromatum guttatum
. On-line liquid chromatography/electrospray ionization-mass spectrometry was used to isolate and quantify the protein. For the identification of the protein, liquid chromatography/electrospray ionization-tandem mass spectrometry analysis of tryptic digests of the protein was carried out. The acquired mass spectra were used for database searching, which led to the identification of a single tryptic peptide. The 12 amino acid tryptic peptide (FLPSEFGNDVDR) was found to be identical to amino acid residues at the positions 108–120 of isoflavone reductase in the
Arabidopsis
genome. A BLAST search identified this sequence region as unique and specific to a class of NAD(P)-dependent reductases involved in phenylpropanoid biosynthesis. Edman degradation revealed that the protein was N-terminally blocked. The amount of the protein (termed RL, NAD(P) reductase-like protein) increased 60-fold from D-4 (4 days before inflorescence-opening, designated as D-day) to D-Day, and declined the following day, when heat-production ceased. When salicylic acid, the endogenous trigger of heat-production in the
Sauromatum
appendix, was applied to premature appendices, a fivefold decrease in the amount of RL was detected in the treated section relative to the non-treated section. About 40 % of RL was found in the cytoplasm. Another 30 % was detected in Percoll-purified mitochondria and the rest, about 30 % was associated with a low speed centrifugation pellet due to nuclei and amyloplast localization. RL was also found in other thermogenic plants and detected in
Arabidopsis
leaves. The function of RL in thermogenic and non-thermogenic plants requires further investigation.</abstract><cop>Boston</cop><pub>Springer US</pub><pmid>23467808</pmid><doi>10.1007/s10930-013-9472-7</doi><tpages>11</tpages></addata></record> |
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subjects | Amino acids Analysis Animal Anatomy Arabidopsis thaliana Araceae - enzymology Araceae - genetics Araceae - growth & development Araceae - metabolism Biochemistry Bioorganic Chemistry Biosynthesis Centrifugation Chemistry Chemistry and Materials Science Cytoplasm Database searching Ethylenediaminetetraacetic acid Flowers & plants Flowers - chemistry Flowers - enzymology Flowers - genetics Flowers - growth & development Genomics Histology Internet/Web search services Ionization Kinetics Liquid chromatography Mass spectra Mass spectrometry Molecular Weight Morphology NAD - metabolism Online searching Organic Chemistry Oxidoreductases - chemistry Oxidoreductases - genetics Oxidoreductases - isolation & purification Oxidoreductases - metabolism Plant biology Plant Components, Aerial - enzymology Plant Components, Aerial - genetics Plant Components, Aerial - metabolism Plant Proteins - chemistry Plant Proteins - genetics Plant Proteins - isolation & purification Plant Proteins - metabolism Povidone Protein Transport Proteins |
title | Purification of a NAD(P) Reductase-Like Protein from the Thermogenic Appendix of the Sauromatum guttatum Inflorescence |
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