new type of mutation in phytochrome A causes enhanced light sensitivity and alters the degradation and subcellular partitioning of the photoreceptor
A specific light program consisting of multiple treatments with alternating red and far-red light pulses was used to isolate mutants in phytochrome A-dependent signal transduction pathways in Arabidopsis. Because of their phenotype, the mutants were called eid for empfindlicher im dunkelroten Licht,...
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description | A specific light program consisting of multiple treatments with alternating red and far-red light pulses was used to isolate mutants in phytochrome A-dependent signal transduction pathways in Arabidopsis. Because of their phenotype, the mutants were called eid for empfindlicher im dunkelroten Licht, which means hypersensitive in far-red light. One of the isolated mutants, eid4, is a novel semi-dominant allele of the phytochrome A gene that carries a missense mutation in the chromophore-binding domain. The mutation did not change the photochemical properties of the photoreceptor, but it leads to an increased stability under light conditions that induce its rapid degradation. Fusion proteins with the green fluorescent protein exhibited clear alterations in subcellular localization of the mutated photoreceptor: The fusion protein was impaired in the formation of sequestered areas of phytochrome in the cytosol, which can explain its reduced light-dependent degradation. In contrast, the mutation stabilizes nuclear speckles (NUS) that appear late under continuous far-red light, whereas the formation of early, transiently appearing NUS remained more or loss unaltered. |
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Because of their phenotype, the mutants were called eid for empfindlicher im dunkelroten Licht, which means hypersensitive in far-red light. One of the isolated mutants, eid4, is a novel semi-dominant allele of the phytochrome A gene that carries a missense mutation in the chromophore-binding domain. The mutation did not change the photochemical properties of the photoreceptor, but it leads to an increased stability under light conditions that induce its rapid degradation. Fusion proteins with the green fluorescent protein exhibited clear alterations in subcellular localization of the mutated photoreceptor: The fusion protein was impaired in the formation of sequestered areas of phytochrome in the cytosol, which can explain its reduced light-dependent degradation. In contrast, the mutation stabilizes nuclear speckles (NUS) that appear late under continuous far-red light, whereas the formation of early, transiently appearing NUS remained more or loss unaltered.</description><identifier>ISSN: 0960-7412</identifier><identifier>EISSN: 1365-313X</identifier><identifier>DOI: 10.1111/j.1365-313x.2004.02286.x</identifier><identifier>PMID: 15610357</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Arabidopsis ; Arabidopsis - genetics ; Arabidopsis Proteins ; Base Sequence ; Biological and medical sciences ; conserved sequences ; far-red light ; Fundamental and applied biological sciences. Psychology ; Genotype & phenotype ; Light ; light intensity ; light signaling ; missense mutation ; Molecular Sequence Data ; Mutation ; Mutation, Missense ; nuclear localization ; nuclear speckles ; Phenotype ; phenotypic variation ; photomorphogenesis ; photoreceptors ; Photosynthesis ; Photosynthetic Reaction Center Complex Proteins - metabolism ; Physical agents ; phytochrome ; Phytochrome - genetics ; Phytochrome - metabolism ; Phytochrome A ; Plant physiology and development ; Plant populations ; protein degradation ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; proteolysis ; recombinant fusion proteins ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Vegetative apparatus, growth and morphogenesis. 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Because of their phenotype, the mutants were called eid for empfindlicher im dunkelroten Licht, which means hypersensitive in far-red light. One of the isolated mutants, eid4, is a novel semi-dominant allele of the phytochrome A gene that carries a missense mutation in the chromophore-binding domain. The mutation did not change the photochemical properties of the photoreceptor, but it leads to an increased stability under light conditions that induce its rapid degradation. Fusion proteins with the green fluorescent protein exhibited clear alterations in subcellular localization of the mutated photoreceptor: The fusion protein was impaired in the formation of sequestered areas of phytochrome in the cytosol, which can explain its reduced light-dependent degradation. In contrast, the mutation stabilizes nuclear speckles (NUS) that appear late under continuous far-red light, whereas the formation of early, transiently appearing NUS remained more or loss unaltered.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Arabidopsis</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis Proteins</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>conserved sequences</subject><subject>far-red light</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genotype & phenotype</subject><subject>Light</subject><subject>light intensity</subject><subject>light signaling</subject><subject>missense mutation</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Mutation, Missense</subject><subject>nuclear localization</subject><subject>nuclear speckles</subject><subject>Phenotype</subject><subject>phenotypic variation</subject><subject>photomorphogenesis</subject><subject>photoreceptors</subject><subject>Photosynthesis</subject><subject>Photosynthetic Reaction Center Complex Proteins - metabolism</subject><subject>Physical agents</subject><subject>phytochrome</subject><subject>Phytochrome - genetics</subject><subject>Phytochrome - metabolism</subject><subject>Phytochrome A</subject><subject>Plant physiology and development</subject><subject>Plant populations</subject><subject>protein degradation</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>proteolysis</subject><subject>recombinant fusion proteins</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Vegetative apparatus, growth and morphogenesis. Senescence</subject><issn>0960-7412</issn><issn>1365-313X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkl2L1DAUhoso7rj6FzQI693UpEnzceHFsvjJgoK74F1Im3SaoW1qkrrT_-EPNnFGFrzREDiB87zngzdFARAsUTqv9yXCtN5ihA9lBSEpYVVxWh4eFJs_iW8Piw0UFG4ZQdVZ8SSEPYSIYUoeF2eopgjimm2Kn5O5A3GdDXAdGJeoonUTsBOY-zW6tvduNOAStGoJJgAz9WpqjQaD3fURBDMFG-0PG1egJg3UEI0PIPYGaLPzSh-r5VRYmtYMwzIoD2blo80ZO-1y28zPvYvOm9bMKTwtHnVqCObZKZ4Xt-_e3lx92F5_fv_x6vJ629aiplvKTSXSrTotmGa6qwkmXUO1EBByWnPaVIR2DadEs1pDhnXVCNIY0QjWdA0-L14d687efV9MiHK0IY-pJuOWICnDmENU_xNEjHBOkUjgy7_AvVv8lJaQFcKEIgRRgvgRar0LwZtOzt6Oyq8SQZn9lXuZbZTZRpn9lb_9lYckfX6qvzSj0ffCk6EJuDgBKrRq6Hzyy4Z7jhImWJ0HfXPk7uxg1v8eQN58-ZRfSf_iqO-Uk2rnU4_br1VaDkLBKU8f7Rcdds0O</recordid><startdate>200501</startdate><enddate>200501</enddate><creator>Dieterle, M</creator><creator>Bauer, D</creator><creator>Buche, C</creator><creator>Krenz, M</creator><creator>Schafer, E</creator><creator>Kretsch, T</creator><general>Blackwell Science Ltd</general><general>Blackwell Science</general><general>Blackwell Publishing Ltd</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>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200501</creationdate><title>new type of mutation in phytochrome A causes enhanced light sensitivity and alters the degradation and subcellular partitioning of the photoreceptor</title><author>Dieterle, M ; Bauer, D ; Buche, C ; Krenz, M ; Schafer, E ; Kretsch, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5956-68e29e292fd97d7df5434fb6d990086586b246fb864d75d073d2b94be9b97bfb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Arabidopsis</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis Proteins</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>conserved sequences</topic><topic>far-red light</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genotype & phenotype</topic><topic>Light</topic><topic>light intensity</topic><topic>light signaling</topic><topic>missense mutation</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Mutation, Missense</topic><topic>nuclear localization</topic><topic>nuclear speckles</topic><topic>Phenotype</topic><topic>phenotypic variation</topic><topic>photomorphogenesis</topic><topic>photoreceptors</topic><topic>Photosynthesis</topic><topic>Photosynthetic Reaction Center Complex Proteins - metabolism</topic><topic>Physical agents</topic><topic>phytochrome</topic><topic>Phytochrome - genetics</topic><topic>Phytochrome - metabolism</topic><topic>Phytochrome A</topic><topic>Plant physiology and development</topic><topic>Plant populations</topic><topic>protein degradation</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>proteolysis</topic><topic>recombinant fusion proteins</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Vegetative apparatus, growth and morphogenesis. Senescence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dieterle, M</creatorcontrib><creatorcontrib>Bauer, D</creatorcontrib><creatorcontrib>Buche, C</creatorcontrib><creatorcontrib>Krenz, M</creatorcontrib><creatorcontrib>Schafer, E</creatorcontrib><creatorcontrib>Kretsch, T</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>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</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>Dieterle, M</au><au>Bauer, D</au><au>Buche, C</au><au>Krenz, M</au><au>Schafer, E</au><au>Kretsch, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>new type of mutation in phytochrome A causes enhanced light sensitivity and alters the degradation and subcellular partitioning of the photoreceptor</atitle><jtitle>The Plant journal : for cell and molecular biology</jtitle><addtitle>Plant J</addtitle><date>2005-01</date><risdate>2005</risdate><volume>41</volume><issue>1</issue><spage>146</spage><epage>161</epage><pages>146-161</pages><issn>0960-7412</issn><eissn>1365-313X</eissn><abstract>A specific light program consisting of multiple treatments with alternating red and far-red light pulses was used to isolate mutants in phytochrome A-dependent signal transduction pathways in Arabidopsis. Because of their phenotype, the mutants were called eid for empfindlicher im dunkelroten Licht, which means hypersensitive in far-red light. One of the isolated mutants, eid4, is a novel semi-dominant allele of the phytochrome A gene that carries a missense mutation in the chromophore-binding domain. The mutation did not change the photochemical properties of the photoreceptor, but it leads to an increased stability under light conditions that induce its rapid degradation. Fusion proteins with the green fluorescent protein exhibited clear alterations in subcellular localization of the mutated photoreceptor: The fusion protein was impaired in the formation of sequestered areas of phytochrome in the cytosol, which can explain its reduced light-dependent degradation. In contrast, the mutation stabilizes nuclear speckles (NUS) that appear late under continuous far-red light, whereas the formation of early, transiently appearing NUS remained more or loss unaltered.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>15610357</pmid><doi>10.1111/j.1365-313x.2004.02286.x</doi><tpages>16</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence amino acid sequences Arabidopsis Arabidopsis - genetics Arabidopsis Proteins Base Sequence Biological and medical sciences conserved sequences far-red light Fundamental and applied biological sciences. Psychology Genotype & phenotype Light light intensity light signaling missense mutation Molecular Sequence Data Mutation Mutation, Missense nuclear localization nuclear speckles Phenotype phenotypic variation photomorphogenesis photoreceptors Photosynthesis Photosynthetic Reaction Center Complex Proteins - metabolism Physical agents phytochrome Phytochrome - genetics Phytochrome - metabolism Phytochrome A Plant physiology and development Plant populations protein degradation Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism proteolysis recombinant fusion proteins Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Vegetative apparatus, growth and morphogenesis. Senescence |
title | new type of mutation in phytochrome A causes enhanced light sensitivity and alters the degradation and subcellular partitioning of the photoreceptor |
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