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Blue Light-Induced Phosphorylation of a Plasma Membrane-Associated Protein in Zea mays L
Blue light induces a variety of photomorphogenic responses in higher plants, among them phototropic curvature, the bending of seedlings toward a unidirectional light source. In dark-grown coleoptiles of maize (Zea mays L.) seedlings, blue light induces rapid phosphorylation of a 114-kD protein at fl...
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Published in: | Plant physiology (Bethesda) 1993-08, Vol.102 (4), p.1211-1218 |
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creator | Julie M. Palmer Short, Timothy W. Gallagher, Sean Briggs, Winslow R. |
description | Blue light induces a variety of photomorphogenic responses in higher plants, among them phototropic curvature, the bending of seedlings toward a unidirectional light source. In dark-grown coleoptiles of maize (Zea mays L.) seedlings, blue light induces rapid phosphorylation of a 114-kD protein at fluence levels that are sufficient to stimulate phototropic curvature. Phosphorylation in response to blue light can be detected in vivo in coleoptile tips preincubated in 32Pi or in vitro in isolated membranes supplemented with [γ-32P]ATP. Phosphorylation reaches a maximum level in vitro within 2 min following an inductive light pulse, but substantial labeling occurs within the first 15 s. Isolated membranes remain activated for several minutes following an in vitro blue light stimulus, even in the absence of exogenous ATP. Phosphoamino acid analysis of the 114-kD protein detected phosphoserine and a trace of phosphothreonine. The kinase involved in phosphorylating the protein in vitro is not dependent on calcium. The 114-kD protein itself has an apparent binding site for ATP, detected by incubating with the nonhydrolyzable analog, 5′-p-fluorosulfonyl-benzoyladenosine. This result suggests that the 114-kD protein, which becomes phosphorylated in response to blue light, may also be capable of kinase activity. |
doi_str_mv | 10.1104/pp.102.4.1211 |
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Palmer ; Short, Timothy W. ; Gallagher, Sean ; Briggs, Winslow R.</creator><creatorcontrib>Julie M. Palmer ; Short, Timothy W. ; Gallagher, Sean ; Briggs, Winslow R.</creatorcontrib><description>Blue light induces a variety of photomorphogenic responses in higher plants, among them phototropic curvature, the bending of seedlings toward a unidirectional light source. In dark-grown coleoptiles of maize (Zea mays L.) seedlings, blue light induces rapid phosphorylation of a 114-kD protein at fluence levels that are sufficient to stimulate phototropic curvature. Phosphorylation in response to blue light can be detected in vivo in coleoptile tips preincubated in 32Pi or in vitro in isolated membranes supplemented with [γ-32P]ATP. Phosphorylation reaches a maximum level in vitro within 2 min following an inductive light pulse, but substantial labeling occurs within the first 15 s. Isolated membranes remain activated for several minutes following an in vitro blue light stimulus, even in the absence of exogenous ATP. Phosphoamino acid analysis of the 114-kD protein detected phosphoserine and a trace of phosphothreonine. The kinase involved in phosphorylating the protein in vitro is not dependent on calcium. The 114-kD protein itself has an apparent binding site for ATP, detected by incubating with the nonhydrolyzable analog, 5′-p-fluorosulfonyl-benzoyladenosine. 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Palmer</creatorcontrib><creatorcontrib>Short, Timothy W.</creatorcontrib><creatorcontrib>Gallagher, Sean</creatorcontrib><creatorcontrib>Briggs, Winslow R.</creatorcontrib><title>Blue Light-Induced Phosphorylation of a Plasma Membrane-Associated Protein in Zea mays L</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>Blue light induces a variety of photomorphogenic responses in higher plants, among them phototropic curvature, the bending of seedlings toward a unidirectional light source. In dark-grown coleoptiles of maize (Zea mays L.) seedlings, blue light induces rapid phosphorylation of a 114-kD protein at fluence levels that are sufficient to stimulate phototropic curvature. Phosphorylation in response to blue light can be detected in vivo in coleoptile tips preincubated in 32Pi or in vitro in isolated membranes supplemented with [γ-32P]ATP. Phosphorylation reaches a maximum level in vitro within 2 min following an inductive light pulse, but substantial labeling occurs within the first 15 s. Isolated membranes remain activated for several minutes following an in vitro blue light stimulus, even in the absence of exogenous ATP. Phosphoamino acid analysis of the 114-kD protein detected phosphoserine and a trace of phosphothreonine. The kinase involved in phosphorylating the protein in vitro is not dependent on calcium. The 114-kD protein itself has an apparent binding site for ATP, detected by incubating with the nonhydrolyzable analog, 5′-p-fluorosulfonyl-benzoyladenosine. This result suggests that the 114-kD protein, which becomes phosphorylated in response to blue light, may also be capable of kinase activity.</description><subject>Biological and medical sciences</subject><subject>Calcium</subject><subject>Cell biochemistry</subject><subject>Cell Biology and Signal Transduction</subject><subject>Cell membranes</subject><subject>Cell physiology</subject><subject>Coleoptiles</subject><subject>Corn</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>Irradiation</subject><subject>Peas</subject><subject>Phosphorylation</subject><subject>Plant physiology and development</subject><subject>Plants</subject><subject>Seedlings</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><recordid>eNpVkU2LFDEQhoMo7rh69CaSgwcvPaaS9HRy8LAufiyMuAcF8RKqk_ROlu5Ob9ItzL83wwyjQkEV1FOfLyEvga0BmHw3TWtgfC3XwAEekRXUgle8luoxWTFWYqaUviDPcr5njIEA-ZRcAOcClN6syM8P_eLpNtzt5upmdIv1jt7uYp52Me17nEMcaewo0tse84D0qx_ahKOvrnKONuB84FOcfRhpsV8e6YD7TLfPyZMO--xfnPwl-fHp4_frL9X22-eb66ttZWvRzJXjGweq9UJutGtdi0wKqVWtbIOcYdvo1pZtHW89NBuslUSUzjbaS92JGsUleX_sOy3t4J3145ywN1MKA6a9iRjM_5kx7Mxd_G2gVpo1pf7tqT7Fh8Xn2QwhW9_35ci4ZAOq1qLRIEVBqyNqU8w5-e48BZg5iGGmqYTcSHMQo_Cv_13tL336fgHenADMFvuuPNaGfOaEEowpVrBXR-w-zzGd05I3dZFT_AHa2JwR</recordid><startdate>19930801</startdate><enddate>19930801</enddate><creator>Julie M. 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Palmer ; Short, Timothy W. ; Gallagher, Sean ; Briggs, Winslow R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c537t-d26d18be3469dbdba04349858c7a20ab79bc122d2be176a584aa4dc79e49f35a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Biological and medical sciences</topic><topic>Calcium</topic><topic>Cell biochemistry</topic><topic>Cell Biology and Signal Transduction</topic><topic>Cell membranes</topic><topic>Cell physiology</topic><topic>Coleoptiles</topic><topic>Corn</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>Irradiation</topic><topic>Peas</topic><topic>Phosphorylation</topic><topic>Plant physiology and development</topic><topic>Plants</topic><topic>Seedlings</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Julie M. Palmer</creatorcontrib><creatorcontrib>Short, Timothy W.</creatorcontrib><creatorcontrib>Gallagher, Sean</creatorcontrib><creatorcontrib>Briggs, Winslow R.</creatorcontrib><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</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>Julie M. Palmer</au><au>Short, Timothy W.</au><au>Gallagher, Sean</au><au>Briggs, Winslow R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Blue Light-Induced Phosphorylation of a Plasma Membrane-Associated Protein in Zea mays L</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>1211</spage><epage>1218</epage><pages>1211-1218</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>Blue light induces a variety of photomorphogenic responses in higher plants, among them phototropic curvature, the bending of seedlings toward a unidirectional light source. In dark-grown coleoptiles of maize (Zea mays L.) seedlings, blue light induces rapid phosphorylation of a 114-kD protein at fluence levels that are sufficient to stimulate phototropic curvature. Phosphorylation in response to blue light can be detected in vivo in coleoptile tips preincubated in 32Pi or in vitro in isolated membranes supplemented with [γ-32P]ATP. Phosphorylation reaches a maximum level in vitro within 2 min following an inductive light pulse, but substantial labeling occurs within the first 15 s. Isolated membranes remain activated for several minutes following an in vitro blue light stimulus, even in the absence of exogenous ATP. Phosphoamino acid analysis of the 114-kD protein detected phosphoserine and a trace of phosphothreonine. The kinase involved in phosphorylating the protein in vitro is not dependent on calcium. The 114-kD protein itself has an apparent binding site for ATP, detected by incubating with the nonhydrolyzable analog, 5′-p-fluorosulfonyl-benzoyladenosine. This result suggests that the 114-kD protein, which becomes phosphorylated in response to blue light, may also be capable of kinase activity.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Physiologists</pub><pmid>12231896</pmid><doi>10.1104/pp.102.4.1211</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Biological and medical sciences Calcium Cell biochemistry Cell Biology and Signal Transduction Cell membranes Cell physiology Coleoptiles Corn Fundamental and applied biological sciences. Psychology Gels Irradiation Peas Phosphorylation Plant physiology and development Plants Seedlings |
title | Blue Light-Induced Phosphorylation of a Plasma Membrane-Associated Protein in Zea mays L |
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