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Phototaxis in the Cyanobacterium Synechocystis sp. PCC 6803: Role of Different Photoreceptors
The second cyanobacterial phytochrome Cph2 from Synechocystis sp. PCC 6803 was suggested as a part of a light-stimulated signal transduction chain inhibiting movement toward blue light. Cph2 has the two bilin binding sites, cysteine-129 and cysteine-1022, that might be involved in sensing of red/far...
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Published in: | Photochemistry and photobiology 2005-11, Vol.81 (6), p.1481-1488 |
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creator | Fiedler, Brita Börner, Thomas Wilde, Annegret |
description | The second cyanobacterial phytochrome Cph2 from Synechocystis sp. PCC 6803 was suggested as a part of a light-stimulated signal transduction chain inhibiting movement toward blue light. Cph2 has the two bilin binding sites, cysteine-129 and cysteine-1022, that might be involved in sensing of red/far-red and blue light, respectively. Here, we present data on wavelength dependence of the phototaxis inhibition under blue light, indicating that Cph2 itself is the photoreceptor for this blue light response. We found that inhibition of blue-light phototaxis in wild-type cells occurred below the transition point of about 470 nm. Substitution of cysteine-1022 with valine led to photomovement of the cells toward blue light (cph2− mutant phenotype). Analysis of mutants lacking cysteine-129 in the N-terminal chromophore binding domain indicated that this domain is also important for Cph2 function or folding of the protein. Furthermore, putative blue-light and phytochrome-like photoreceptors encoded by the Synechocystis sp. PCC 6803 genome were inactivated in wild-type and cph2 knockout mutant background. Our results suggest that none of these potential photoreceptors interfere with Cph2 function, although inactivation of taxD1 as well as slr1694 encoding a BLUF protein led to cells that reversed the direction of movement under blue light illumination in mutant strains of cph2. |
doi_str_mv | 10.1562/2005-06-28-RA-592 |
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Substitution of cysteine-1022 with valine led to photomovement of the cells toward blue light (cph2− mutant phenotype). Analysis of mutants lacking cysteine-129 in the N-terminal chromophore binding domain indicated that this domain is also important for Cph2 function or folding of the protein. Furthermore, putative blue-light and phytochrome-like photoreceptors encoded by the Synechocystis sp. PCC 6803 genome were inactivated in wild-type and cph2 knockout mutant background. Our results suggest that none of these potential photoreceptors interfere with Cph2 function, although inactivation of taxD1 as well as slr1694 encoding a BLUF protein led to cells that reversed the direction of movement under blue light illumination in mutant strains of cph2.</description><identifier>ISSN: 0031-8655</identifier><identifier>EISSN: 1751-1097</identifier><identifier>DOI: 10.1562/2005-06-28-RA-592</identifier><identifier>PMID: 16354116</identifier><identifier>CODEN: PHCBAP</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Bacterial Proteins - genetics ; Cryptochromes ; Cyanophyta ; Flavoproteins - genetics ; Flavoproteins - radiation effects ; Light ; Models, Biological ; Movement - radiation effects ; Mutation ; Photic Stimulation ; Photochemistry ; Photoreceptors, Microbial - classification ; Photoreceptors, Microbial - genetics ; Photoreceptors, Microbial - physiology ; Phytochrome - genetics ; Research s ; Synechocystis ; Synechocystis - genetics ; Synechocystis - physiology ; Synechocystis - radiation effects</subject><ispartof>Photochemistry and photobiology, 2005-11, Vol.81 (6), p.1481-1488</ispartof><rights>American Society for Photobiology</rights><rights>Copyright American Society for Photobiology Nov/Dec 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-b4821-616419726b658fa65569ecb1635610081788db425c883bd10ef1b3c950499f6e3</citedby><cites>FETCH-LOGICAL-b4821-616419726b658fa65569ecb1635610081788db425c883bd10ef1b3c950499f6e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16354116$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fiedler, Brita</creatorcontrib><creatorcontrib>Börner, Thomas</creatorcontrib><creatorcontrib>Wilde, Annegret</creatorcontrib><title>Phototaxis in the Cyanobacterium Synechocystis sp. PCC 6803: Role of Different Photoreceptors</title><title>Photochemistry and photobiology</title><addtitle>Photochem Photobiol</addtitle><description>The second cyanobacterial phytochrome Cph2 from Synechocystis sp. PCC 6803 was suggested as a part of a light-stimulated signal transduction chain inhibiting movement toward blue light. Cph2 has the two bilin binding sites, cysteine-129 and cysteine-1022, that might be involved in sensing of red/far-red and blue light, respectively. Here, we present data on wavelength dependence of the phototaxis inhibition under blue light, indicating that Cph2 itself is the photoreceptor for this blue light response. We found that inhibition of blue-light phototaxis in wild-type cells occurred below the transition point of about 470 nm. Substitution of cysteine-1022 with valine led to photomovement of the cells toward blue light (cph2− mutant phenotype). Analysis of mutants lacking cysteine-129 in the N-terminal chromophore binding domain indicated that this domain is also important for Cph2 function or folding of the protein. Furthermore, putative blue-light and phytochrome-like photoreceptors encoded by the Synechocystis sp. PCC 6803 genome were inactivated in wild-type and cph2 knockout mutant background. Our results suggest that none of these potential photoreceptors interfere with Cph2 function, although inactivation of taxD1 as well as slr1694 encoding a BLUF protein led to cells that reversed the direction of movement under blue light illumination in mutant strains of cph2.</description><subject>Bacterial Proteins - genetics</subject><subject>Cryptochromes</subject><subject>Cyanophyta</subject><subject>Flavoproteins - genetics</subject><subject>Flavoproteins - radiation effects</subject><subject>Light</subject><subject>Models, Biological</subject><subject>Movement - radiation effects</subject><subject>Mutation</subject><subject>Photic Stimulation</subject><subject>Photochemistry</subject><subject>Photoreceptors, Microbial - classification</subject><subject>Photoreceptors, Microbial - genetics</subject><subject>Photoreceptors, Microbial - physiology</subject><subject>Phytochrome - genetics</subject><subject>Research s</subject><subject>Synechocystis</subject><subject>Synechocystis - genetics</subject><subject>Synechocystis - physiology</subject><subject>Synechocystis - radiation effects</subject><issn>0031-8655</issn><issn>1751-1097</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqNkcFu1DAURS0EokPhA9ggiwU7t35O7NjsRoHOgCqIBhArZCWZF01KJh7sRDR_X08zAolNWb3NOVf36RLyEvgFSCUuBeeSccWEZpslk0Y8IgvIJDDgJntMFpwnwLSS8ow8C-GGc0hNBk_JGahEpgBqQX4UOze4obxtA217OuyQ5lPZu6qsB_TtuKdfph7rnaunMEQmHC5okedUaZ68pRvXIXUNfdc2DXrsB3of57HGQzzhOXnSlF3AF6d7Tr5dvf-ar9n159WHfHnNqlQLYApUCiYTqlJSN2UsrAzW1bGlAs41ZFpvq1TIWuuk2gLHBqqkNpKnxjQKk3PyZs49ePdrxDDYfRtq7LqyRzcGq7Q2Uqb8QRCMAZkZHcHX_4A3bvR9fMKKJBOQGG4iBDNUexeCx8YefLsv_WSB2-NC9riQ5coKbTdLGxeKzqtT8FjtcfvXOE0SATUDv9sOp4cTbbEuINUQRTaLbRjw9o9Y-p9WZUkm7fdPKwsb_fGqWK3t8cXLma9a53r8j-53U2a2qA</recordid><startdate>200511</startdate><enddate>200511</enddate><creator>Fiedler, Brita</creator><creator>Börner, Thomas</creator><creator>Wilde, Annegret</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</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>3V.</scope><scope>4T-</scope><scope>7RV</scope><scope>7TM</scope><scope>7U7</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>S0X</scope><scope>F1W</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>200511</creationdate><title>Phototaxis in the Cyanobacterium Synechocystis sp. 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Academic</collection><jtitle>Photochemistry and photobiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fiedler, Brita</au><au>Börner, Thomas</au><au>Wilde, Annegret</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phototaxis in the Cyanobacterium Synechocystis sp. PCC 6803: Role of Different Photoreceptors</atitle><jtitle>Photochemistry and photobiology</jtitle><addtitle>Photochem Photobiol</addtitle><date>2005-11</date><risdate>2005</risdate><volume>81</volume><issue>6</issue><spage>1481</spage><epage>1488</epage><pages>1481-1488</pages><issn>0031-8655</issn><eissn>1751-1097</eissn><coden>PHCBAP</coden><abstract>The second cyanobacterial phytochrome Cph2 from Synechocystis sp. PCC 6803 was suggested as a part of a light-stimulated signal transduction chain inhibiting movement toward blue light. Cph2 has the two bilin binding sites, cysteine-129 and cysteine-1022, that might be involved in sensing of red/far-red and blue light, respectively. Here, we present data on wavelength dependence of the phototaxis inhibition under blue light, indicating that Cph2 itself is the photoreceptor for this blue light response. We found that inhibition of blue-light phototaxis in wild-type cells occurred below the transition point of about 470 nm. Substitution of cysteine-1022 with valine led to photomovement of the cells toward blue light (cph2− mutant phenotype). Analysis of mutants lacking cysteine-129 in the N-terminal chromophore binding domain indicated that this domain is also important for Cph2 function or folding of the protein. Furthermore, putative blue-light and phytochrome-like photoreceptors encoded by the Synechocystis sp. PCC 6803 genome were inactivated in wild-type and cph2 knockout mutant background. Our results suggest that none of these potential photoreceptors interfere with Cph2 function, although inactivation of taxD1 as well as slr1694 encoding a BLUF protein led to cells that reversed the direction of movement under blue light illumination in mutant strains of cph2.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>16354116</pmid><doi>10.1562/2005-06-28-RA-592</doi><tpages>8</tpages></addata></record> |
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subjects | Bacterial Proteins - genetics Cryptochromes Cyanophyta Flavoproteins - genetics Flavoproteins - radiation effects Light Models, Biological Movement - radiation effects Mutation Photic Stimulation Photochemistry Photoreceptors, Microbial - classification Photoreceptors, Microbial - genetics Photoreceptors, Microbial - physiology Phytochrome - genetics Research s Synechocystis Synechocystis - genetics Synechocystis - physiology Synechocystis - radiation effects |
title | Phototaxis in the Cyanobacterium Synechocystis sp. PCC 6803: Role of Different Photoreceptors |
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