Identification of a major soluble protein in mitochondria from nonphotosynthetic tissues as NAD-dependent formate dehydrogenase
In many plant species, one of the most abundant soluble proteins (as judged by two-dimensional polyacrylamide gel electrophoresis) in mitochondria from nongreen tissues is a 40-kD polypeptide that is relatively scarce in mitochondria from photosynthetic tissues. cDNA sequences encoding this polypept...
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| Veröffentlicht in: | Plant physiology (Bethesda) 1993-08, Vol.102 (4), p.1171-1177 |
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| creator | COLAS DES FRANCS-SMALL, C AMBARD-BRETTEVILLE, F SMALL, I. D REMY, R |
| description | In many plant species, one of the most abundant soluble proteins (as judged by two-dimensional polyacrylamide gel electrophoresis) in mitochondria from nongreen tissues is a 40-kD polypeptide that is relatively scarce in mitochondria from photosynthetic tissues. cDNA sequences encoding this polypeptide were isolated from a lambda gt11 cDNA expression library from potato (Solanum tuberosum L.) by screening with a specific antibody raised against the 40-kD polypeptide. The cDNA sequence contains an open reading frame of 1137 nucleotides whose predicted amino acid sequence shows strong homology to an NAD-dependent formate dehydrogenase (EC 1.2.1.2) from Pseudomonas sp. 101. Comparison of the cDNA sequence with the N-terminal amino acid sequence of the mature 40-kD polypeptide suggests that the polypeptide is made as a precursor with a 23-amino acid presequence that shows characteristics typical of mitochondrial targeting signals. The identity of the polypeptide was confirmed by assaying the formate dehydrogenase activity in plant mitochondria from various tissues and by activity staining of mitochondrial proteins run on native gels combined with antibody recognition. The abundance and distribution of this protein suggest that higher plant mitochondria from various nonphotosynthetic plant tissues (tubers, storage roots, seeds, dark-grown shoots, cauliflower heads, and tissues grown in vitro) might contain a formate-producing fermentation pathway similar to those described in bacteria and algae. |
| doi_str_mv | 10.1104/pp.102.4.1171 |
| format | Article |
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D ; REMY, R</creator><creatorcontrib>COLAS DES FRANCS-SMALL, C ; AMBARD-BRETTEVILLE, F ; SMALL, I. D ; REMY, R</creatorcontrib><description>In many plant species, one of the most abundant soluble proteins (as judged by two-dimensional polyacrylamide gel electrophoresis) in mitochondria from nongreen tissues is a 40-kD polypeptide that is relatively scarce in mitochondria from photosynthetic tissues. cDNA sequences encoding this polypeptide were isolated from a lambda gt11 cDNA expression library from potato (Solanum tuberosum L.) by screening with a specific antibody raised against the 40-kD polypeptide. The cDNA sequence contains an open reading frame of 1137 nucleotides whose predicted amino acid sequence shows strong homology to an NAD-dependent formate dehydrogenase (EC 1.2.1.2) from Pseudomonas sp. 101. Comparison of the cDNA sequence with the N-terminal amino acid sequence of the mature 40-kD polypeptide suggests that the polypeptide is made as a precursor with a 23-amino acid presequence that shows characteristics typical of mitochondrial targeting signals. The identity of the polypeptide was confirmed by assaying the formate dehydrogenase activity in plant mitochondria from various tissues and by activity staining of mitochondrial proteins run on native gels combined with antibody recognition. The abundance and distribution of this protein suggest that higher plant mitochondria from various nonphotosynthetic plant tissues (tubers, storage roots, seeds, dark-grown shoots, cauliflower heads, and tissues grown in vitro) might contain a formate-producing fermentation pathway similar to those described in bacteria and algae.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.102.4.1171</identifier><identifier>PMID: 8278546</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Physiologists</publisher><subject>Amino Acid Sequence ; Amino acids ; arn mensajero ; arn messager ; Base Sequence ; Biological and medical sciences ; Cloning, Molecular ; Complementary DNA ; Dehydrogenases ; Enzymes ; expresion genica ; expression des genes ; Formate Dehydrogenases - analysis ; Formate Dehydrogenases - biosynthesis ; Formate Dehydrogenases - genetics ; Formates ; Fundamental and applied biological sciences. Psychology ; Gels ; gene expression ; Gene Library ; Genetics ; graine ; Life Sciences ; messenger rna ; Metabolism ; Mitochondria ; Mitochondria - enzymology ; mitochondrie ; mitocondria ; Molecular Biology and Gene Regulation ; Molecular Sequence Data ; NAD - metabolism ; nucleotide sequence ; oxidoreductases ; oxidorreductasas ; oxydoreductase ; Photosynthesis ; Plant physiology and development ; Plant tissues ; Plants ; Plants genetics ; Pseudomonas - enzymology ; racine ; raices ; roots ; secuencia nucleica ; seeds ; semilla ; Sequence Homology, Amino Acid ; sequence nucleique ; solanum tuberosum ; Solanum tuberosum - enzymology ; tubercule ; tuberculo ; Tubers</subject><ispartof>Plant physiology (Bethesda), 1993-08, Vol.102 (4), p.1171-1177</ispartof><rights>Copyright 1993 American Society of Plant Physiologists</rights><rights>1994 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c591t-852c45019c2d0e2a12a5da4ebee37c4b1e0a4704abb832441e4fccfdd10e96e93</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4275309$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4275309$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,803,885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3830076$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8278546$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02706845$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>COLAS DES FRANCS-SMALL, C</creatorcontrib><creatorcontrib>AMBARD-BRETTEVILLE, F</creatorcontrib><creatorcontrib>SMALL, I. D</creatorcontrib><creatorcontrib>REMY, R</creatorcontrib><title>Identification of a major soluble protein in mitochondria from nonphotosynthetic tissues as NAD-dependent formate dehydrogenase</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>In many plant species, one of the most abundant soluble proteins (as judged by two-dimensional polyacrylamide gel electrophoresis) in mitochondria from nongreen tissues is a 40-kD polypeptide that is relatively scarce in mitochondria from photosynthetic tissues. cDNA sequences encoding this polypeptide were isolated from a lambda gt11 cDNA expression library from potato (Solanum tuberosum L.) by screening with a specific antibody raised against the 40-kD polypeptide. The cDNA sequence contains an open reading frame of 1137 nucleotides whose predicted amino acid sequence shows strong homology to an NAD-dependent formate dehydrogenase (EC 1.2.1.2) from Pseudomonas sp. 101. Comparison of the cDNA sequence with the N-terminal amino acid sequence of the mature 40-kD polypeptide suggests that the polypeptide is made as a precursor with a 23-amino acid presequence that shows characteristics typical of mitochondrial targeting signals. The identity of the polypeptide was confirmed by assaying the formate dehydrogenase activity in plant mitochondria from various tissues and by activity staining of mitochondrial proteins run on native gels combined with antibody recognition. The abundance and distribution of this protein suggest that higher plant mitochondria from various nonphotosynthetic plant tissues (tubers, storage roots, seeds, dark-grown shoots, cauliflower heads, and tissues grown in vitro) might contain a formate-producing fermentation pathway similar to those described in bacteria and algae.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>arn mensajero</subject><subject>arn messager</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>Complementary DNA</subject><subject>Dehydrogenases</subject><subject>Enzymes</subject><subject>expresion genica</subject><subject>expression des genes</subject><subject>Formate Dehydrogenases - analysis</subject><subject>Formate Dehydrogenases - biosynthesis</subject><subject>Formate Dehydrogenases - genetics</subject><subject>Formates</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>gene expression</subject><subject>Gene Library</subject><subject>Genetics</subject><subject>graine</subject><subject>Life Sciences</subject><subject>messenger rna</subject><subject>Metabolism</subject><subject>Mitochondria</subject><subject>Mitochondria - enzymology</subject><subject>mitochondrie</subject><subject>mitocondria</subject><subject>Molecular Biology and Gene Regulation</subject><subject>Molecular Sequence Data</subject><subject>NAD - metabolism</subject><subject>nucleotide sequence</subject><subject>oxidoreductases</subject><subject>oxidorreductasas</subject><subject>oxydoreductase</subject><subject>Photosynthesis</subject><subject>Plant physiology and development</subject><subject>Plant tissues</subject><subject>Plants</subject><subject>Plants genetics</subject><subject>Pseudomonas - enzymology</subject><subject>racine</subject><subject>raices</subject><subject>roots</subject><subject>secuencia nucleica</subject><subject>seeds</subject><subject>semilla</subject><subject>Sequence Homology, Amino Acid</subject><subject>sequence nucleique</subject><subject>solanum tuberosum</subject><subject>Solanum tuberosum - enzymology</subject><subject>tubercule</subject><subject>tuberculo</subject><subject>Tubers</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUGP0zAQhSMEWrqFIzdAPiAkDikex26SA4dqF9iVKjjAni3HmTSuEjvY7ko98ddx1KoCJEse-30zY8_LsldAVwCUf5ymFVC24ulUwpNsAaJgORO8epotKE0xrar6eXYdwp5SCgXwq-yqYmUl-HqR_b5v0UbTGa2icZa4jigyqr3zJLjh0AxIJu8iGkvSGk10une29UaRzruRWGen3kUXjjb2GI0m0YRwwEBUIN82t3mLE9q5B-mcH1VE0mJ_bL3boVUBX2TPOjUEfHnel9nDl88_b-7y7fev9zebba5FDTGvBNNcUKg1aykyBUyJVnFsEItS8waQKl5SrpqmKhjngLzTumtboFivsS6W2adT3enQjNjq9CCvBjl5Myp_lE4Z-a9iTS937lGCqGrKUv6HU37_X9bdZivnO8pKuq64eITEvj_38u5XGkWUowkah0FZdIcgyzUIJpJPyyw_gdq7EDx2l8pA5WyunKYUMsnlbG7i3_z9iQt9djPp7866CloNnVdWm3DBiqqgtJyx1ydsH6LzF5mzUhR0HtXbk9wpJ9XOpwoPP6CuOQVaAkDxB2tHwso</recordid><startdate>19930801</startdate><enddate>19930801</enddate><creator>COLAS DES FRANCS-SMALL, C</creator><creator>AMBARD-BRETTEVILLE, F</creator><creator>SMALL, I. D</creator><creator>REMY, R</creator><general>American Society of Plant Physiologists</general><general>Oxford University Press ; American Society of Plant Biologists</general><scope>FBQ</scope><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>7X8</scope><scope>1XC</scope><scope>5PM</scope></search><sort><creationdate>19930801</creationdate><title>Identification of a major soluble protein in mitochondria from nonphotosynthetic tissues as NAD-dependent formate dehydrogenase</title><author>COLAS DES FRANCS-SMALL, C ; AMBARD-BRETTEVILLE, F ; SMALL, I. D ; REMY, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c591t-852c45019c2d0e2a12a5da4ebee37c4b1e0a4704abb832441e4fccfdd10e96e93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>arn mensajero</topic><topic>arn messager</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>Complementary DNA</topic><topic>Dehydrogenases</topic><topic>Enzymes</topic><topic>expresion genica</topic><topic>expression des genes</topic><topic>Formate Dehydrogenases - analysis</topic><topic>Formate Dehydrogenases - biosynthesis</topic><topic>Formate Dehydrogenases - genetics</topic><topic>Formates</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>gene expression</topic><topic>Gene Library</topic><topic>Genetics</topic><topic>graine</topic><topic>Life Sciences</topic><topic>messenger rna</topic><topic>Metabolism</topic><topic>Mitochondria</topic><topic>Mitochondria - enzymology</topic><topic>mitochondrie</topic><topic>mitocondria</topic><topic>Molecular Biology and Gene Regulation</topic><topic>Molecular Sequence Data</topic><topic>NAD - metabolism</topic><topic>nucleotide sequence</topic><topic>oxidoreductases</topic><topic>oxidorreductasas</topic><topic>oxydoreductase</topic><topic>Photosynthesis</topic><topic>Plant physiology and development</topic><topic>Plant tissues</topic><topic>Plants</topic><topic>Plants genetics</topic><topic>Pseudomonas - enzymology</topic><topic>racine</topic><topic>raices</topic><topic>roots</topic><topic>secuencia nucleica</topic><topic>seeds</topic><topic>semilla</topic><topic>Sequence Homology, Amino Acid</topic><topic>sequence nucleique</topic><topic>solanum tuberosum</topic><topic>Solanum tuberosum - enzymology</topic><topic>tubercule</topic><topic>tuberculo</topic><topic>Tubers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>COLAS DES FRANCS-SMALL, C</creatorcontrib><creatorcontrib>AMBARD-BRETTEVILLE, F</creatorcontrib><creatorcontrib>SMALL, I. D</creatorcontrib><creatorcontrib>REMY, R</creatorcontrib><collection>AGRIS</collection><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>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>COLAS DES FRANCS-SMALL, C</au><au>AMBARD-BRETTEVILLE, F</au><au>SMALL, I. D</au><au>REMY, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of a major soluble protein in mitochondria from nonphotosynthetic tissues as NAD-dependent formate dehydrogenase</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>1993-08-01</date><risdate>1993</risdate><volume>102</volume><issue>4</issue><spage>1171</spage><epage>1177</epage><pages>1171-1177</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>In many plant species, one of the most abundant soluble proteins (as judged by two-dimensional polyacrylamide gel electrophoresis) in mitochondria from nongreen tissues is a 40-kD polypeptide that is relatively scarce in mitochondria from photosynthetic tissues. cDNA sequences encoding this polypeptide were isolated from a lambda gt11 cDNA expression library from potato (Solanum tuberosum L.) by screening with a specific antibody raised against the 40-kD polypeptide. The cDNA sequence contains an open reading frame of 1137 nucleotides whose predicted amino acid sequence shows strong homology to an NAD-dependent formate dehydrogenase (EC 1.2.1.2) from Pseudomonas sp. 101. Comparison of the cDNA sequence with the N-terminal amino acid sequence of the mature 40-kD polypeptide suggests that the polypeptide is made as a precursor with a 23-amino acid presequence that shows characteristics typical of mitochondrial targeting signals. The identity of the polypeptide was confirmed by assaying the formate dehydrogenase activity in plant mitochondria from various tissues and by activity staining of mitochondrial proteins run on native gels combined with antibody recognition. The abundance and distribution of this protein suggest that higher plant mitochondria from various nonphotosynthetic plant tissues (tubers, storage roots, seeds, dark-grown shoots, cauliflower heads, and tissues grown in vitro) might contain a formate-producing fermentation pathway similar to those described in bacteria and algae.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>8278546</pmid><doi>10.1104/pp.102.4.1171</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Amino acids arn mensajero arn messager Base Sequence Biological and medical sciences Cloning, Molecular Complementary DNA Dehydrogenases Enzymes expresion genica expression des genes Formate Dehydrogenases - analysis Formate Dehydrogenases - biosynthesis Formate Dehydrogenases - genetics Formates Fundamental and applied biological sciences. Psychology Gels gene expression Gene Library Genetics graine Life Sciences messenger rna Metabolism Mitochondria Mitochondria - enzymology mitochondrie mitocondria Molecular Biology and Gene Regulation Molecular Sequence Data NAD - metabolism nucleotide sequence oxidoreductases oxidorreductasas oxydoreductase Photosynthesis Plant physiology and development Plant tissues Plants Plants genetics Pseudomonas - enzymology racine raices roots secuencia nucleica seeds semilla Sequence Homology, Amino Acid sequence nucleique solanum tuberosum Solanum tuberosum - enzymology tubercule tuberculo Tubers |
| title | Identification of a major soluble protein in mitochondria from nonphotosynthetic tissues as NAD-dependent formate dehydrogenase |
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