Arabidopsis nph1 and npl1: Blue Light Receptors That Mediate Both Phototropism and Chloroplast Relocation
UV-A/blue light acts to regulate a number of physiological processes in higher plants. These include light-driven chloroplast movement and phototropism. The NPH1 gene of Arabidopsis encodes an autophosphorylating protein kinase that functions as a photoreceptor for phototropism in response to low-in...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2001-06, Vol.98 (12), p.6969-6974 |
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creator | Sakai, Tatsuya Kagawa, Takatoshi Kasahara, Masahiro Swartz, Trevor E. Christie, John M. Briggs, Winslow R. Wada, Masamitsu Okada, Kiyotaka |
description | UV-A/blue light acts to regulate a number of physiological processes in higher plants. These include light-driven chloroplast movement and phototropism. The NPH1 gene of Arabidopsis encodes an autophosphorylating protein kinase that functions as a photoreceptor for phototropism in response to low-intensity blue light. However, nph1 mutants have been reported to exhibit normal phototropic curvature under high-intensity blue light, indicating the presence of an additional phototropic receptor. A likely candidate is the nph1 homologue, npl1, which has recently been shown to mediate the avoidance response of chloroplasts to high-intensity blue light in Arabidopsis. Here we demonstrate that npl1, like nph1, noncovalently binds the chromophore flavin mononucleotide (FMN) within two specialized PAS domains, termed LOV domains. Furthermore, when expressed in insect cells, npl1, like nph1, undergoes light-dependent autophosphorylation, indicating that npl1 also functions as a light receptor kinase. Consistent with this conclusion, we show that a nph1 npl1 double mutant exhibits an impaired phototropic response under both low- and high-intensity blue light. Hence, npl1 functions as a second phototropic receptor under high fluence rate conditions and is, in part, functionally redundant to nph1. We also demonstrate that both chloroplast accumulation in response to low-intensity light and chloroplast avoidance movement in response to high-intensity light are lacking in the nph1 npl1 double mutant. Our findings therefore indicate that nph1 and npl1 show partially overlapping functions in two different responses, phototropism and chloroplast relocation, in a fluence rate-dependent manner. |
doi_str_mv | 10.1073/pnas.101137598 |
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These include light-driven chloroplast movement and phototropism. The NPH1 gene of Arabidopsis encodes an autophosphorylating protein kinase that functions as a photoreceptor for phototropism in response to low-intensity blue light. However, nph1 mutants have been reported to exhibit normal phototropic curvature under high-intensity blue light, indicating the presence of an additional phototropic receptor. A likely candidate is the nph1 homologue, npl1, which has recently been shown to mediate the avoidance response of chloroplasts to high-intensity blue light in Arabidopsis. Here we demonstrate that npl1, like nph1, noncovalently binds the chromophore flavin mononucleotide (FMN) within two specialized PAS domains, termed LOV domains. Furthermore, when expressed in insect cells, npl1, like nph1, undergoes light-dependent autophosphorylation, indicating that npl1 also functions as a light receptor kinase. Consistent with this conclusion, we show that a nph1 npl1 double mutant exhibits an impaired phototropic response under both low- and high-intensity blue light. Hence, npl1 functions as a second phototropic receptor under high fluence rate conditions and is, in part, functionally redundant to nph1. We also demonstrate that both chloroplast accumulation in response to low-intensity light and chloroplast avoidance movement in response to high-intensity light are lacking in the nph1 npl1 double mutant. Our findings therefore indicate that nph1 and npl1 show partially overlapping functions in two different responses, phototropism and chloroplast relocation, in a fluence rate-dependent manner.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.101137598</identifier><identifier>PMID: 11371609</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Arabidopsis ; Arabidopsis - metabolism ; Arabidopsis - physiology ; Arabidopsis Proteins ; Biological Sciences ; Chloroplasts ; Chloroplasts - physiology ; Curvature ; Flowers & plants ; Fluence ; Genes ; Hypocotyls ; Light ; Mutation ; nph1 gene ; nphl1 gene ; Phosphoproteins - metabolism ; Photoreceptors ; Photosynthetic Reaction Center Complex Proteins - metabolism ; Phototropism ; Physiological regulation ; Plant cells ; Plant Proteins - metabolism ; Proteins ; Receptors ; Recombinant Proteins - metabolism ; Space life sciences</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2001-06, Vol.98 (12), p.6969-6974</ispartof><rights>Copyright 1993-2001 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jun 5, 2001</rights><rights>Copyright © 2001, The National Academy of Sciences 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c518t-74681e9009200737c06c815979d2f92b5b175bfa306f0ba1c2d3a0ae1272c1df3</citedby><cites>FETCH-LOGICAL-c518t-74681e9009200737c06c815979d2f92b5b175bfa306f0ba1c2d3a0ae1272c1df3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/98/12.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3055921$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3055921$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11371609$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sakai, Tatsuya</creatorcontrib><creatorcontrib>Kagawa, Takatoshi</creatorcontrib><creatorcontrib>Kasahara, Masahiro</creatorcontrib><creatorcontrib>Swartz, Trevor E.</creatorcontrib><creatorcontrib>Christie, John M.</creatorcontrib><creatorcontrib>Briggs, Winslow R.</creatorcontrib><creatorcontrib>Wada, Masamitsu</creatorcontrib><creatorcontrib>Okada, Kiyotaka</creatorcontrib><title>Arabidopsis nph1 and npl1: Blue Light Receptors That Mediate Both Phototropism and Chloroplast Relocation</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>UV-A/blue light acts to regulate a number of physiological processes in higher plants. These include light-driven chloroplast movement and phototropism. The NPH1 gene of Arabidopsis encodes an autophosphorylating protein kinase that functions as a photoreceptor for phototropism in response to low-intensity blue light. However, nph1 mutants have been reported to exhibit normal phototropic curvature under high-intensity blue light, indicating the presence of an additional phototropic receptor. A likely candidate is the nph1 homologue, npl1, which has recently been shown to mediate the avoidance response of chloroplasts to high-intensity blue light in Arabidopsis. Here we demonstrate that npl1, like nph1, noncovalently binds the chromophore flavin mononucleotide (FMN) within two specialized PAS domains, termed LOV domains. Furthermore, when expressed in insect cells, npl1, like nph1, undergoes light-dependent autophosphorylation, indicating that npl1 also functions as a light receptor kinase. Consistent with this conclusion, we show that a nph1 npl1 double mutant exhibits an impaired phototropic response under both low- and high-intensity blue light. Hence, npl1 functions as a second phototropic receptor under high fluence rate conditions and is, in part, functionally redundant to nph1. We also demonstrate that both chloroplast accumulation in response to low-intensity light and chloroplast avoidance movement in response to high-intensity light are lacking in the nph1 npl1 double mutant. Our findings therefore indicate that nph1 and npl1 show partially overlapping functions in two different responses, phototropism and chloroplast relocation, in a fluence rate-dependent manner.</description><subject>Arabidopsis</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis - physiology</subject><subject>Arabidopsis Proteins</subject><subject>Biological Sciences</subject><subject>Chloroplasts</subject><subject>Chloroplasts - physiology</subject><subject>Curvature</subject><subject>Flowers & plants</subject><subject>Fluence</subject><subject>Genes</subject><subject>Hypocotyls</subject><subject>Light</subject><subject>Mutation</subject><subject>nph1 gene</subject><subject>nphl1 gene</subject><subject>Phosphoproteins - metabolism</subject><subject>Photoreceptors</subject><subject>Photosynthetic Reaction Center Complex Proteins - metabolism</subject><subject>Phototropism</subject><subject>Physiological regulation</subject><subject>Plant cells</subject><subject>Plant Proteins - metabolism</subject><subject>Proteins</subject><subject>Receptors</subject><subject>Recombinant Proteins - metabolism</subject><subject>Space life sciences</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkk1v1DAQhiMEokvhygmhiAM9pcw4H7YRl3ZVPqRFIFTOluM4jVfeONgOgn-Pwy5L4QDywWPN845n_DrLHiOcI9DyxTTKkCLEktac3clWCByLpuJwN1sBEFqwilQn2YMQtgDAawb3s5MFxwb4KjMXXramc1MwIR-nAXM5dimw-DK_tLPON-ZmiPknrfQUnQ_59SBj_l53RkadX7o45B8HF130bjJh91O9HqxLRyvDIrROyWjc-DC710sb9KPDfpp9fn11vX5bbD68ebe-2BSqRhYLWjUMNU-tEkgDUgWNYlhzyjvSc9LWLdK67WUJTQ-tREW6UoLUSChR2PXlafZqX3ea253ulB6jl1ZM3uyk_y6cNOLPzGgGceO-irKqGpLkzw9y777MOkSxM0Fpa-Wo3RwEBcYpq6v_gkgZJ1hiAp_9BW7d7Mf0BoIAVpDWcu35HlLeheB1f2wYQSxOi8VpcXQ6CZ7eHvM3frD2FrAIf6U5E0hEw5sFOPsnIPrZ2qi_xUQ-2ZPbkP7AES2hrpcRfwA2BcXu</recordid><startdate>20010605</startdate><enddate>20010605</enddate><creator>Sakai, Tatsuya</creator><creator>Kagawa, Takatoshi</creator><creator>Kasahara, Masahiro</creator><creator>Swartz, Trevor E.</creator><creator>Christie, John M.</creator><creator>Briggs, Winslow R.</creator><creator>Wada, Masamitsu</creator><creator>Okada, Kiyotaka</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><general>The National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20010605</creationdate><title>Arabidopsis nph1 and npl1: Blue Light Receptors That Mediate Both Phototropism and Chloroplast Relocation</title><author>Sakai, Tatsuya ; 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These include light-driven chloroplast movement and phototropism. The NPH1 gene of Arabidopsis encodes an autophosphorylating protein kinase that functions as a photoreceptor for phototropism in response to low-intensity blue light. However, nph1 mutants have been reported to exhibit normal phototropic curvature under high-intensity blue light, indicating the presence of an additional phototropic receptor. A likely candidate is the nph1 homologue, npl1, which has recently been shown to mediate the avoidance response of chloroplasts to high-intensity blue light in Arabidopsis. Here we demonstrate that npl1, like nph1, noncovalently binds the chromophore flavin mononucleotide (FMN) within two specialized PAS domains, termed LOV domains. Furthermore, when expressed in insect cells, npl1, like nph1, undergoes light-dependent autophosphorylation, indicating that npl1 also functions as a light receptor kinase. Consistent with this conclusion, we show that a nph1 npl1 double mutant exhibits an impaired phototropic response under both low- and high-intensity blue light. Hence, npl1 functions as a second phototropic receptor under high fluence rate conditions and is, in part, functionally redundant to nph1. We also demonstrate that both chloroplast accumulation in response to low-intensity light and chloroplast avoidance movement in response to high-intensity light are lacking in the nph1 npl1 double mutant. Our findings therefore indicate that nph1 and npl1 show partially overlapping functions in two different responses, phototropism and chloroplast relocation, in a fluence rate-dependent manner.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>11371609</pmid><doi>10.1073/pnas.101137598</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Arabidopsis Arabidopsis - metabolism Arabidopsis - physiology Arabidopsis Proteins Biological Sciences Chloroplasts Chloroplasts - physiology Curvature Flowers & plants Fluence Genes Hypocotyls Light Mutation nph1 gene nphl1 gene Phosphoproteins - metabolism Photoreceptors Photosynthetic Reaction Center Complex Proteins - metabolism Phototropism Physiological regulation Plant cells Plant Proteins - metabolism Proteins Receptors Recombinant Proteins - metabolism Space life sciences |
title | Arabidopsis nph1 and npl1: Blue Light Receptors That Mediate Both Phototropism and Chloroplast Relocation |
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