Developmental expression and biochemical analysis of the Arabidopsis atao1 gene encoding an H2O2‐generating diamine oxidase
Summary A copper amine oxidase encoding gene, atao1, has been isolated and characterized from Arabidopsis thaliana. Sequence analysis reveals that atao1 encodes a 668 amino acid polypeptide (ATAO1) with 48% identity to copper amine oxidases from pea and lentil. The promoter region of atao1 was trans...
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| Veröffentlicht in: | The Plant journal : for cell and molecular biology 1998-03, Vol.13 (6), p.781-791 |
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| container_title | The Plant journal : for cell and molecular biology |
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| creator | Møller, Simon G. McPherson, Michael J. |
| description | Summary
A copper amine oxidase encoding gene, atao1, has been isolated and characterized from Arabidopsis thaliana. Sequence analysis reveals that atao1 encodes a 668 amino acid polypeptide (ATAO1) with 48% identity to copper amine oxidases from pea and lentil. The promoter region of atao1 was transcriptionally fused with the reporter genes encoding β‐glucuronidase and modified green fluorescent protein. Analysis of transgenic Arabidopsis together with in situ hybridization of wild‐type plants reveals temporally and spatially discrete patterns of gene expression in lateral root cap cells, vascular tissue of roots, developing leaves, the hypocotyl, and in the style/stigmatal tissue. Enzyme activity assays show that ATAO1 preferentially oxidizes the aliphatic diamine putrescine with production of the corresponding aldehyde, ammonia and hydrogen peroxide, a recognized plant signal molecule and substrate for peroxidases. Histochemical analysis reveals that atao1 expression in developing tracheary elements precedes and overlaps with lignification and therefore is a good marker for vascular development. In both vascular tissue and the root cap, atao1 expression occurs in cells destined to undergo programmed cell death. |
| doi_str_mv | 10.1046/j.1365-313X.1998.00080.x |
| format | Article |
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A copper amine oxidase encoding gene, atao1, has been isolated and characterized from Arabidopsis thaliana. Sequence analysis reveals that atao1 encodes a 668 amino acid polypeptide (ATAO1) with 48% identity to copper amine oxidases from pea and lentil. The promoter region of atao1 was transcriptionally fused with the reporter genes encoding β‐glucuronidase and modified green fluorescent protein. Analysis of transgenic Arabidopsis together with in situ hybridization of wild‐type plants reveals temporally and spatially discrete patterns of gene expression in lateral root cap cells, vascular tissue of roots, developing leaves, the hypocotyl, and in the style/stigmatal tissue. Enzyme activity assays show that ATAO1 preferentially oxidizes the aliphatic diamine putrescine with production of the corresponding aldehyde, ammonia and hydrogen peroxide, a recognized plant signal molecule and substrate for peroxidases. Histochemical analysis reveals that atao1 expression in developing tracheary elements precedes and overlaps with lignification and therefore is a good marker for vascular development. In both vascular tissue and the root cap, atao1 expression occurs in cells destined to undergo programmed cell death.</description><identifier>ISSN: 0960-7412</identifier><identifier>EISSN: 1365-313X</identifier><identifier>DOI: 10.1046/j.1365-313X.1998.00080.x</identifier><identifier>PMID: 9681017</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science, Ltd</publisher><subject>Amine Oxidase (Copper-Containing) - genetics ; Amine Oxidase (Copper-Containing) - metabolism ; Amino Acid Sequence ; Apoptosis ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Arabidopsis - growth & development ; Base Sequence ; Biological and medical sciences ; Cell Wall - metabolism ; Cloning, Molecular ; Cross-Linking Reagents ; DNA Primers - genetics ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Developmental ; Gene Expression Regulation, Enzymologic ; Genes, Plant ; Hydrogen Peroxide - metabolism ; In Situ Hybridization ; Metabolism ; Molecular Sequence Data ; Plant physiology and development ; Plant Roots - enzymology ; Plants, Genetically Modified ; Sequence Homology, Amino Acid ; Substrate Specificity</subject><ispartof>The Plant journal : for cell and molecular biology, 1998-03, Vol.13 (6), p.781-791</ispartof><rights>1998 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4590-bda064a12e71c33bd3cad522fb3e79e2828c79540e91dbd840bc39c65cfc3fae3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1365-313X.1998.00080.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45575,46833</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2251615$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9681017$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Møller, Simon G.</creatorcontrib><creatorcontrib>McPherson, Michael J.</creatorcontrib><title>Developmental expression and biochemical analysis of the Arabidopsis atao1 gene encoding an H2O2‐generating diamine oxidase</title><title>The Plant journal : for cell and molecular biology</title><addtitle>Plant J</addtitle><description>Summary
A copper amine oxidase encoding gene, atao1, has been isolated and characterized from Arabidopsis thaliana. Sequence analysis reveals that atao1 encodes a 668 amino acid polypeptide (ATAO1) with 48% identity to copper amine oxidases from pea and lentil. The promoter region of atao1 was transcriptionally fused with the reporter genes encoding β‐glucuronidase and modified green fluorescent protein. Analysis of transgenic Arabidopsis together with in situ hybridization of wild‐type plants reveals temporally and spatially discrete patterns of gene expression in lateral root cap cells, vascular tissue of roots, developing leaves, the hypocotyl, and in the style/stigmatal tissue. Enzyme activity assays show that ATAO1 preferentially oxidizes the aliphatic diamine putrescine with production of the corresponding aldehyde, ammonia and hydrogen peroxide, a recognized plant signal molecule and substrate for peroxidases. Histochemical analysis reveals that atao1 expression in developing tracheary elements precedes and overlaps with lignification and therefore is a good marker for vascular development. In both vascular tissue and the root cap, atao1 expression occurs in cells destined to undergo programmed cell death.</description><subject>Amine Oxidase (Copper-Containing) - genetics</subject><subject>Amine Oxidase (Copper-Containing) - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Apoptosis</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - growth & development</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cell Wall - metabolism</subject><subject>Cloning, Molecular</subject><subject>Cross-Linking Reagents</subject><subject>DNA Primers - genetics</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Genes, Plant</subject><subject>Hydrogen Peroxide - metabolism</subject><subject>In Situ Hybridization</subject><subject>Metabolism</subject><subject>Molecular Sequence Data</subject><subject>Plant physiology and development</subject><subject>Plant Roots - enzymology</subject><subject>Plants, Genetically Modified</subject><subject>Sequence Homology, Amino Acid</subject><subject>Substrate Specificity</subject><issn>0960-7412</issn><issn>1365-313X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kctu1DAUhi0EKkPhEZC8QOwSju3cLLGpyqWgSmVRJHbWiX3SepTEIc7AzAKJR-AZeRIcOpqVj__v01mcnzEuIBdQVG-2uVBVmSmhvuVC6yYHgAby_SO2OYHHbAO6gqwuhHzKnsW4BRC1qoozdqarRqTPhv16Rz-oD9NA44I9p_00U4w-jBxHx1sf7D0N3iaEI_aH6CMPHV_uiV_M2HoXpjXCBYPgdzQSp9EG58e75PMreSP__v6z5jMua-g8Dj5ZYe8dRnrOnnTYR3pxfM_Z1w_vby-vsuubj58uL64zW5QastYhVAUKSbWwSrVOWXSllF2rqNYkG9nYWpcFkBaudU0BrVXaVqXtrOqQ1Dl7_bB3msP3HcXFDD5a6nscKeyiaQBkDYVI4sujuGsHcmaa_YDzwRzvlfirI8eYjtLNOFofT5qUpahEmbS3D9pP39PhhAWYtT2zNWtJZi3JrO2Z_-2Zvbn98jkN6h9Nn5C6</recordid><startdate>199803</startdate><enddate>199803</enddate><creator>Møller, Simon G.</creator><creator>McPherson, Michael J.</creator><general>Blackwell Science, Ltd</general><general>Blackwell Science</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>199803</creationdate><title>Developmental expression and biochemical analysis of the Arabidopsis atao1 gene encoding an H2O2‐generating diamine oxidase</title><author>Møller, Simon G. ; McPherson, Michael J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4590-bda064a12e71c33bd3cad522fb3e79e2828c79540e91dbd840bc39c65cfc3fae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amine Oxidase (Copper-Containing) - genetics</topic><topic>Amine Oxidase (Copper-Containing) - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Apoptosis</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - growth & development</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cell Wall - metabolism</topic><topic>Cloning, Molecular</topic><topic>Cross-Linking Reagents</topic><topic>DNA Primers - genetics</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Developmental</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Genes, Plant</topic><topic>Hydrogen Peroxide - metabolism</topic><topic>In Situ Hybridization</topic><topic>Metabolism</topic><topic>Molecular Sequence Data</topic><topic>Plant physiology and development</topic><topic>Plant Roots - enzymology</topic><topic>Plants, Genetically Modified</topic><topic>Sequence Homology, Amino Acid</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Møller, Simon G.</creatorcontrib><creatorcontrib>McPherson, Michael J.</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>MEDLINE - Academic</collection><jtitle>The Plant journal : for cell and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Møller, Simon G.</au><au>McPherson, Michael J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Developmental expression and biochemical analysis of the Arabidopsis atao1 gene encoding an H2O2‐generating diamine oxidase</atitle><jtitle>The Plant journal : for cell and molecular biology</jtitle><addtitle>Plant J</addtitle><date>1998-03</date><risdate>1998</risdate><volume>13</volume><issue>6</issue><spage>781</spage><epage>791</epage><pages>781-791</pages><issn>0960-7412</issn><eissn>1365-313X</eissn><abstract>Summary
A copper amine oxidase encoding gene, atao1, has been isolated and characterized from Arabidopsis thaliana. Sequence analysis reveals that atao1 encodes a 668 amino acid polypeptide (ATAO1) with 48% identity to copper amine oxidases from pea and lentil. The promoter region of atao1 was transcriptionally fused with the reporter genes encoding β‐glucuronidase and modified green fluorescent protein. Analysis of transgenic Arabidopsis together with in situ hybridization of wild‐type plants reveals temporally and spatially discrete patterns of gene expression in lateral root cap cells, vascular tissue of roots, developing leaves, the hypocotyl, and in the style/stigmatal tissue. Enzyme activity assays show that ATAO1 preferentially oxidizes the aliphatic diamine putrescine with production of the corresponding aldehyde, ammonia and hydrogen peroxide, a recognized plant signal molecule and substrate for peroxidases. Histochemical analysis reveals that atao1 expression in developing tracheary elements precedes and overlaps with lignification and therefore is a good marker for vascular development. In both vascular tissue and the root cap, atao1 expression occurs in cells destined to undergo programmed cell death.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science, Ltd</pub><pmid>9681017</pmid><doi>10.1046/j.1365-313X.1998.00080.x</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amine Oxidase (Copper-Containing) - genetics Amine Oxidase (Copper-Containing) - metabolism Amino Acid Sequence Apoptosis Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis - growth & development Base Sequence Biological and medical sciences Cell Wall - metabolism Cloning, Molecular Cross-Linking Reagents DNA Primers - genetics Enzymes Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Developmental Gene Expression Regulation, Enzymologic Genes, Plant Hydrogen Peroxide - metabolism In Situ Hybridization Metabolism Molecular Sequence Data Plant physiology and development Plant Roots - enzymology Plants, Genetically Modified Sequence Homology, Amino Acid Substrate Specificity |
| title | Developmental expression and biochemical analysis of the Arabidopsis atao1 gene encoding an H2O2‐generating diamine oxidase |
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