Independent evolution of the prochlorophyte and green plant chlorophyll a/b light-harvesting proteins
The prochlorophytes are oxygenic prokaryotes differing from other cyanobacteria by the presence of a light-harvesting system containing both chlorophylls (Chls) a and b and by the absence of phycobilins. We demonstrate here that the Chl a/b binding proteins from all three known prochlorophyte genera...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1996-12, Vol.93 (26), p.15244-15248 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | La Roche, J. (Brookhaven National Laboratory, Upton, NY.) Staay, G.W.M. van der Partensky, F Ducret, A Aebersold, R Li, R Golden, S.S Hiller, R.G Wrench, P.M Larkum, A.W.D |
| description | The prochlorophytes are oxygenic prokaryotes differing from other cyanobacteria by the presence of a light-harvesting system containing both chlorophylls (Chls) a and b and by the absence of phycobilins. We demonstrate here that the Chl a/b binding proteins from all three known prochlorophyte genera are closely related to IsiA, a cyanobacterial Chl a-binding protein induced by iron starvation, and to CP43, a constitutively expressed Chl a antenna protein of photosystem II. The prochlorophyte Chl a/b protein (pcb) genes do not belong to the extended gene family encoding eukaryotic Chl a/b and Chl a/c light-harvesting proteins. Although higher plants and prochlorophytes share common pigment complements, their light-harvesting systems have evolved independently |
| doi_str_mv | 10.1073/pnas.93.26.15244 |
| format | Article |
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(Brookhaven National Laboratory, Upton, NY.) ; Staay, G.W.M. van der ; Partensky, F ; Ducret, A ; Aebersold, R ; Li, R ; Golden, S.S ; Hiller, R.G ; Wrench, P.M ; Larkum, A.W.D</creator><creatorcontrib>La Roche, J. (Brookhaven National Laboratory, Upton, NY.) ; Staay, G.W.M. van der ; Partensky, F ; Ducret, A ; Aebersold, R ; Li, R ; Golden, S.S ; Hiller, R.G ; Wrench, P.M ; Larkum, A.W.D</creatorcontrib><description>The prochlorophytes are oxygenic prokaryotes differing from other cyanobacteria by the presence of a light-harvesting system containing both chlorophylls (Chls) a and b and by the absence of phycobilins. We demonstrate here that the Chl a/b binding proteins from all three known prochlorophyte genera are closely related to IsiA, a cyanobacterial Chl a-binding protein induced by iron starvation, and to CP43, a constitutively expressed Chl a antenna protein of photosystem II. The prochlorophyte Chl a/b protein (pcb) genes do not belong to the extended gene family encoding eukaryotic Chl a/b and Chl a/c light-harvesting proteins. Although higher plants and prochlorophytes share common pigment complements, their light-harvesting systems have evolved independently</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.93.26.15244</identifier><identifier>PMID: 8986795</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; Antennas ; Base Sequence ; Biological Sciences ; Carrier proteins ; Chlorophyll ; CHLOROPHYLLE ; Chlorophylls ; Chloroplasts ; CLOROFILAS ; Cyanobacteria ; Cyanobacteria - chemistry ; Cyanobacteria - genetics ; CYANOPHYTA ; Evolution ; Flowers & plants ; GENE ; GENES ; Genes, Plant ; Light-Harvesting Protein Complexes ; Molecular Sequence Data ; Photosynthetic Reaction Center Complex Proteins - chemistry ; Photosynthetic Reaction Center Complex Proteins - genetics ; Photosystem II Protein Complex ; Phycobilins ; Phylogeny ; Pigments ; Plants ; Plants - genetics ; PROTEINAS AGLUTINANTES ; PROTEINE DE LIAISON ; Proteins ; SECUENCIA NUCLEOTIDICA ; Sequence Homology, Amino Acid ; SEQUENCE NUCLEOTIDIQUE ; Space life sciences</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1996-12, Vol.93 (26), p.15244-15248</ispartof><rights>Copyright 1996 National Academy of Sciences</rights><rights>Copyright National Academy of Sciences Dec 24, 1996</rights><rights>Copyright © 1996, The National Academy of Sciences of the USA 1996</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c511t-3fb2cf9142dd1d4592571fbf8531e756e40a6e08e743163600eecc85f92613a83</citedby><cites>FETCH-LOGICAL-c511t-3fb2cf9142dd1d4592571fbf8531e756e40a6e08e743163600eecc85f92613a83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/93/26.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/40860$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/40860$$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/8986795$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>La Roche, J. (Brookhaven National Laboratory, Upton, NY.)</creatorcontrib><creatorcontrib>Staay, G.W.M. van der</creatorcontrib><creatorcontrib>Partensky, F</creatorcontrib><creatorcontrib>Ducret, A</creatorcontrib><creatorcontrib>Aebersold, R</creatorcontrib><creatorcontrib>Li, R</creatorcontrib><creatorcontrib>Golden, S.S</creatorcontrib><creatorcontrib>Hiller, R.G</creatorcontrib><creatorcontrib>Wrench, P.M</creatorcontrib><creatorcontrib>Larkum, A.W.D</creatorcontrib><title>Independent evolution of the prochlorophyte and green plant chlorophyll a/b light-harvesting proteins</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The prochlorophytes are oxygenic prokaryotes differing from other cyanobacteria by the presence of a light-harvesting system containing both chlorophylls (Chls) a and b and by the absence of phycobilins. We demonstrate here that the Chl a/b binding proteins from all three known prochlorophyte genera are closely related to IsiA, a cyanobacterial Chl a-binding protein induced by iron starvation, and to CP43, a constitutively expressed Chl a antenna protein of photosystem II. The prochlorophyte Chl a/b protein (pcb) genes do not belong to the extended gene family encoding eukaryotic Chl a/b and Chl a/c light-harvesting proteins. Although higher plants and prochlorophytes share common pigment complements, their light-harvesting systems have evolved independently</description><subject>Amino Acid Sequence</subject><subject>Antennas</subject><subject>Base Sequence</subject><subject>Biological Sciences</subject><subject>Carrier proteins</subject><subject>Chlorophyll</subject><subject>CHLOROPHYLLE</subject><subject>Chlorophylls</subject><subject>Chloroplasts</subject><subject>CLOROFILAS</subject><subject>Cyanobacteria</subject><subject>Cyanobacteria - chemistry</subject><subject>Cyanobacteria - genetics</subject><subject>CYANOPHYTA</subject><subject>Evolution</subject><subject>Flowers & plants</subject><subject>GENE</subject><subject>GENES</subject><subject>Genes, Plant</subject><subject>Light-Harvesting Protein Complexes</subject><subject>Molecular Sequence Data</subject><subject>Photosynthetic Reaction Center Complex Proteins - chemistry</subject><subject>Photosynthetic Reaction Center Complex Proteins - genetics</subject><subject>Photosystem II Protein Complex</subject><subject>Phycobilins</subject><subject>Phylogeny</subject><subject>Pigments</subject><subject>Plants</subject><subject>Plants - genetics</subject><subject>PROTEINAS AGLUTINANTES</subject><subject>PROTEINE DE LIAISON</subject><subject>Proteins</subject><subject>SECUENCIA NUCLEOTIDICA</subject><subject>Sequence Homology, Amino Acid</subject><subject>SEQUENCE NUCLEOTIDIQUE</subject><subject>Space life sciences</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUtv1DAUhSMEKtPCHiEhoi4Qm0z9fkhsUMWjUiUW0LXlSW4eI08cbGdE_z0OMwyUBRvfxfnO9T06RfECozVGkl5No41rTddErDEnjD0qVhhpXAmm0eNihRCRlWKEPS3OY9wihDRX6Kw4U1oJqfmqgJuxgQnyM6YS9t7NafBj6dsy9VBOwde988FP_X2C0o5N2QWAsZyczfxJc660V5vSDV2fqt6GPcQ0jN3iTzCM8VnxpLUuwvPjvCjuPn74dv25uv3y6eb6_W1Vc4xTRdsNqVuNGWka3DCuCZe43bSKUwySC2DICkAKJKNYUIEQQF0r3moiMLWKXhTvDnunebODps6hgnVmCsPOhnvj7WAeKuPQm87vDRFULfY3R3vw3-ecweyGWIPLYcHP0UglmBSSZPDyH3Dr5zDmaIYgTDGnjGcIHaA6-BgDtKc7MDJLe2Zpz2iafze_2suWV3_ffzIc68r666O-OH-rDze8_T9h2tm5BD9SRl8e0G1MPpxYhpRAf8TWemO7MERz91VLJASj9CeMusH-</recordid><startdate>19961224</startdate><enddate>19961224</enddate><creator>La Roche, J. 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(Brookhaven National Laboratory, Upton, NY.)</au><au>Staay, G.W.M. van der</au><au>Partensky, F</au><au>Ducret, A</au><au>Aebersold, R</au><au>Li, R</au><au>Golden, S.S</au><au>Hiller, R.G</au><au>Wrench, P.M</au><au>Larkum, A.W.D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Independent evolution of the prochlorophyte and green plant chlorophyll a/b light-harvesting proteins</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1996-12-24</date><risdate>1996</risdate><volume>93</volume><issue>26</issue><spage>15244</spage><epage>15248</epage><pages>15244-15248</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The prochlorophytes are oxygenic prokaryotes differing from other cyanobacteria by the presence of a light-harvesting system containing both chlorophylls (Chls) a and b and by the absence of phycobilins. We demonstrate here that the Chl a/b binding proteins from all three known prochlorophyte genera are closely related to IsiA, a cyanobacterial Chl a-binding protein induced by iron starvation, and to CP43, a constitutively expressed Chl a antenna protein of photosystem II. The prochlorophyte Chl a/b protein (pcb) genes do not belong to the extended gene family encoding eukaryotic Chl a/b and Chl a/c light-harvesting proteins. Although higher plants and prochlorophytes share common pigment complements, their light-harvesting systems have evolved independently</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>8986795</pmid><doi>10.1073/pnas.93.26.15244</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1996-12, Vol.93 (26), p.15244-15248 |
| issn | 0027-8424 1091-6490 |
| language | eng |
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| source | MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; JSTOR |
| subjects | Amino Acid Sequence Antennas Base Sequence Biological Sciences Carrier proteins Chlorophyll CHLOROPHYLLE Chlorophylls Chloroplasts CLOROFILAS Cyanobacteria Cyanobacteria - chemistry Cyanobacteria - genetics CYANOPHYTA Evolution Flowers & plants GENE GENES Genes, Plant Light-Harvesting Protein Complexes Molecular Sequence Data Photosynthetic Reaction Center Complex Proteins - chemistry Photosynthetic Reaction Center Complex Proteins - genetics Photosystem II Protein Complex Phycobilins Phylogeny Pigments Plants Plants - genetics PROTEINAS AGLUTINANTES PROTEINE DE LIAISON Proteins SECUENCIA NUCLEOTIDICA Sequence Homology, Amino Acid SEQUENCE NUCLEOTIDIQUE Space life sciences |
| title | Independent evolution of the prochlorophyte and green plant chlorophyll a/b light-harvesting proteins |
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