Evolutionary significance of an algal gene encoding an [FeFe]-hydrogenase with F-domain homology and hydrogenase activity in Chlorella variabilis NC64A
[FeFe]-hydrogenases (HYDA) link the production of molecular H2 to anaerobic metabolism in many green algae. Similar to Chlamydomonas reinhardtii, Chlorella variabilis NC64A (Trebouxiophyceae, Chlorophyta) exhibits [FeFe]-hydrogenase (HYDA) activity during anoxia. In contrast to C. reinhardtii and ot...
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| Veröffentlicht in: | Planta 2011-10, Vol.234 (4), p.829-843 |
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| creator | Meuser, Jonathan E. Boyd, Eric S. Ananyev, Gennady Karns, Devin Radakovits, Randor Murthy, U. M. Narayana Ghirardi, Maria L. Dismukes, G. Charles Peters, John W. Posewitz, Matthew C. |
| description | [FeFe]-hydrogenases (HYDA) link the production of molecular H2 to anaerobic metabolism in many green algae. Similar to Chlamydomonas reinhardtii, Chlorella variabilis NC64A (Trebouxiophyceae, Chlorophyta) exhibits [FeFe]-hydrogenase (HYDA) activity during anoxia. In contrast to C. reinhardtii and other chlorophycean algae, which contain hydrogenases with only the HYDA active site (H-cluster), C. variabilis NC64A is the only known green alga containing HYDA genes encoding accessory FeS cluster-binding domains (F-cluster). cDNA sequencing confirmed the presence of F-cluster HYDA1 mRNA transcripts, and identified deviations from the in silico splicing models. We show that HYDA activity in C. variabilis NC64A is coupled to anoxic photosynthetic electron transport (PSII linked, as well as PSII-independent) and dark fermentation. We also show that the in vivo H2-photoproduction activity observed is as O2 sensitive as in C. reinhardtii. The two C. variabilis NC64A HYDA sequences are similar to homologs found in more deeply branching bacteria (Thermotogales), diatoms, and heterotrophic flagellates, suggesting that an F-cluster HYDA is the ancestral enzyme in algae. Phylogenetic analysis indicates that the algal HYDA H-cluster domains are monophyletic, suggesting that they share a common origin, and evolved from a single ancestral F-cluster HYDA. Furthermore, phylogenetic reconstruction indicates that the multiple algal HYDA paralogs are the result of gene duplication events that occurred independently within each algal lineage. Collectively, comparative genomic, physiological, and phylogenetic analyses of the C. variabilis NC64A hydrogenase has provided new insights into the molecular evolution and diversity of algal [FeFe]-hydrogenases. |
| doi_str_mv | 10.1007/s00425-011-1431-y |
| format | Article |
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M. Narayana ; Ghirardi, Maria L. ; Dismukes, G. Charles ; Peters, John W. ; Posewitz, Matthew C.</creator><creatorcontrib>Meuser, Jonathan E. ; Boyd, Eric S. ; Ananyev, Gennady ; Karns, Devin ; Radakovits, Randor ; Murthy, U. M. Narayana ; Ghirardi, Maria L. ; Dismukes, G. Charles ; Peters, John W. ; Posewitz, Matthew C. ; National Renewable Energy Lab. (NREL), Golden, CO (United States)</creatorcontrib><description>[FeFe]-hydrogenases (HYDA) link the production of molecular H2 to anaerobic metabolism in many green algae. Similar to Chlamydomonas reinhardtii, Chlorella variabilis NC64A (Trebouxiophyceae, Chlorophyta) exhibits [FeFe]-hydrogenase (HYDA) activity during anoxia. In contrast to C. reinhardtii and other chlorophycean algae, which contain hydrogenases with only the HYDA active site (H-cluster), C. variabilis NC64A is the only known green alga containing HYDA genes encoding accessory FeS cluster-binding domains (F-cluster). cDNA sequencing confirmed the presence of F-cluster HYDA1 mRNA transcripts, and identified deviations from the in silico splicing models. We show that HYDA activity in C. variabilis NC64A is coupled to anoxic photosynthetic electron transport (PSII linked, as well as PSII-independent) and dark fermentation. We also show that the in vivo H2-photoproduction activity observed is as O2 sensitive as in C. reinhardtii. The two C. variabilis NC64A HYDA sequences are similar to homologs found in more deeply branching bacteria (Thermotogales), diatoms, and heterotrophic flagellates, suggesting that an F-cluster HYDA is the ancestral enzyme in algae. Phylogenetic analysis indicates that the algal HYDA H-cluster domains are monophyletic, suggesting that they share a common origin, and evolved from a single ancestral F-cluster HYDA. Furthermore, phylogenetic reconstruction indicates that the multiple algal HYDA paralogs are the result of gene duplication events that occurred independently within each algal lineage. Collectively, comparative genomic, physiological, and phylogenetic analyses of the C. variabilis NC64A hydrogenase has provided new insights into the molecular evolution and diversity of algal [FeFe]-hydrogenases.</description><identifier>ISSN: 0032-0935</identifier><identifier>EISSN: 1432-2048</identifier><identifier>DOI: 10.1007/s00425-011-1431-y</identifier><identifier>PMID: 21643991</identifier><identifier>CODEN: PLANAB</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer</publisher><subject>Agriculture ; ALGAE ; Amino Acid Sequence ; Anaerobiosis ; ANOXIA ; Aquatic plants ; BACTERIA ; Base Sequence ; BASIC BIOLOGICAL SCIENCES ; Biological and medical sciences ; Biomedical and Life Sciences ; Cell Hypoxia ; CHLAMYDOMONAS ; Chlamydomonas reinhardtii - enzymology ; Chlamydomonas reinhardtii - genetics ; Chlamydomonas reinhardtii - metabolism ; CHLORELLA ; Chlorella - enzymology ; Chlorella - genetics ; Chlorella - metabolism ; chlorella variablilis NC64A ; Chlorophyll - metabolism ; Complementary DNA ; Culture Media ; Darkness ; DIATOMS ; DNA, Complementary - genetics ; DNA, Plant - genetics ; Ecology ; ELECTRONS ; ENZYMES ; Evolution ; Evolution, Molecular ; F-cluster domain ; FERMENTATION ; Forestry ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Enzymologic - genetics ; Gene Expression Regulation, Plant ; GENES ; Genomes ; Genomics ; Green algae ; HYDA ; Hydrogen - metabolism ; Hydrogenase - genetics ; Hydrogenase - metabolism ; HYDROGENASES ; IN VIVO ; INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY ; Iron sulfides ; Iron-Sulfur Proteins - genetics ; Iron-Sulfur Proteins - metabolism ; Life Sciences ; Light ; METABOLISM ; Molecular Sequence Data ; NAD - metabolism ; ORIGIN ; Original Article ; Oxidation-Reduction ; Oxygen - metabolism ; Phylogenetics ; Phylogeny ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Plant Sciences ; PRODUCTION ; Recombinant Proteins ; RNA, Plant - genetics ; SPLICING ; Sugars ; Time Factors ; TRANSPORT</subject><ispartof>Planta, 2011-10, Vol.234 (4), p.829-843</ispartof><rights>Springer-Verlag 2011</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c449t-4eb2f421b1cbaa795bb92b42002e5261582c5be439ae1687d662e0d97d4c8a8c3</citedby><cites>FETCH-LOGICAL-c449t-4eb2f421b1cbaa795bb92b42002e5261582c5be439ae1687d662e0d97d4c8a8c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/23884646$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/23884646$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27901,27902,41464,42533,51294,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24570603$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21643991$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1036398$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Meuser, Jonathan E.</creatorcontrib><creatorcontrib>Boyd, Eric S.</creatorcontrib><creatorcontrib>Ananyev, Gennady</creatorcontrib><creatorcontrib>Karns, Devin</creatorcontrib><creatorcontrib>Radakovits, Randor</creatorcontrib><creatorcontrib>Murthy, U. M. Narayana</creatorcontrib><creatorcontrib>Ghirardi, Maria L.</creatorcontrib><creatorcontrib>Dismukes, G. Charles</creatorcontrib><creatorcontrib>Peters, John W.</creatorcontrib><creatorcontrib>Posewitz, Matthew C.</creatorcontrib><creatorcontrib>National Renewable Energy Lab. (NREL), Golden, CO (United States)</creatorcontrib><title>Evolutionary significance of an algal gene encoding an [FeFe]-hydrogenase with F-domain homology and hydrogenase activity in Chlorella variabilis NC64A</title><title>Planta</title><addtitle>Planta</addtitle><addtitle>Planta</addtitle><description>[FeFe]-hydrogenases (HYDA) link the production of molecular H2 to anaerobic metabolism in many green algae. Similar to Chlamydomonas reinhardtii, Chlorella variabilis NC64A (Trebouxiophyceae, Chlorophyta) exhibits [FeFe]-hydrogenase (HYDA) activity during anoxia. In contrast to C. reinhardtii and other chlorophycean algae, which contain hydrogenases with only the HYDA active site (H-cluster), C. variabilis NC64A is the only known green alga containing HYDA genes encoding accessory FeS cluster-binding domains (F-cluster). cDNA sequencing confirmed the presence of F-cluster HYDA1 mRNA transcripts, and identified deviations from the in silico splicing models. We show that HYDA activity in C. variabilis NC64A is coupled to anoxic photosynthetic electron transport (PSII linked, as well as PSII-independent) and dark fermentation. We also show that the in vivo H2-photoproduction activity observed is as O2 sensitive as in C. reinhardtii. The two C. variabilis NC64A HYDA sequences are similar to homologs found in more deeply branching bacteria (Thermotogales), diatoms, and heterotrophic flagellates, suggesting that an F-cluster HYDA is the ancestral enzyme in algae. Phylogenetic analysis indicates that the algal HYDA H-cluster domains are monophyletic, suggesting that they share a common origin, and evolved from a single ancestral F-cluster HYDA. Furthermore, phylogenetic reconstruction indicates that the multiple algal HYDA paralogs are the result of gene duplication events that occurred independently within each algal lineage. Collectively, comparative genomic, physiological, and phylogenetic analyses of the C. variabilis NC64A hydrogenase has provided new insights into the molecular evolution and diversity of algal [FeFe]-hydrogenases.</description><subject>Agriculture</subject><subject>ALGAE</subject><subject>Amino Acid Sequence</subject><subject>Anaerobiosis</subject><subject>ANOXIA</subject><subject>Aquatic plants</subject><subject>BACTERIA</subject><subject>Base Sequence</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Hypoxia</subject><subject>CHLAMYDOMONAS</subject><subject>Chlamydomonas reinhardtii - enzymology</subject><subject>Chlamydomonas reinhardtii - genetics</subject><subject>Chlamydomonas reinhardtii - metabolism</subject><subject>CHLORELLA</subject><subject>Chlorella - enzymology</subject><subject>Chlorella - genetics</subject><subject>Chlorella - metabolism</subject><subject>chlorella variablilis NC64A</subject><subject>Chlorophyll - metabolism</subject><subject>Complementary DNA</subject><subject>Culture Media</subject><subject>Darkness</subject><subject>DIATOMS</subject><subject>DNA, Complementary - genetics</subject><subject>DNA, Plant - genetics</subject><subject>Ecology</subject><subject>ELECTRONS</subject><subject>ENZYMES</subject><subject>Evolution</subject><subject>Evolution, Molecular</subject><subject>F-cluster domain</subject><subject>FERMENTATION</subject><subject>Forestry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Enzymologic - genetics</subject><subject>Gene Expression Regulation, Plant</subject><subject>GENES</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Green algae</subject><subject>HYDA</subject><subject>Hydrogen - metabolism</subject><subject>Hydrogenase - genetics</subject><subject>Hydrogenase - metabolism</subject><subject>HYDROGENASES</subject><subject>IN VIVO</subject><subject>INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY</subject><subject>Iron sulfides</subject><subject>Iron-Sulfur Proteins - genetics</subject><subject>Iron-Sulfur Proteins - metabolism</subject><subject>Life Sciences</subject><subject>Light</subject><subject>METABOLISM</subject><subject>Molecular Sequence Data</subject><subject>NAD - metabolism</subject><subject>ORIGIN</subject><subject>Original Article</subject><subject>Oxidation-Reduction</subject><subject>Oxygen - metabolism</subject><subject>Phylogenetics</subject><subject>Phylogeny</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Plant Sciences</subject><subject>PRODUCTION</subject><subject>Recombinant Proteins</subject><subject>RNA, Plant - genetics</subject><subject>SPLICING</subject><subject>Sugars</subject><subject>Time Factors</subject><subject>TRANSPORT</subject><issn>0032-0935</issn><issn>1432-2048</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kc9u1DAQxi0EokvhATiArEqIU8B2HMc5Vqtui1TBBU4IRY4zSbzK2sV2FuVJeF0cZely4uSR5zff_PkQek3JB0pI-TEQwlmREUozynOazU_QJgUsY4TLp2hDSIpJlRcX6EUIe0JSsiyfowtGBc-rim7Q75ujG6donFV-xsH01nRGK6sBuw4ri9XYqxH3YAGD1a41tl--v-9gBz-yYW69S0kVAP8yccC7rHUHZSwe3MGNrp8T3OJ_MaWjOZo44wRth9F5GEeFj8ob1ZjRBPx5K_j1S_SsU2OAV6f3En3b3Xzd3mX3X24_ba_vM815FTMODes4ow3VjVJlVTRNxRrOCGFQMEELyXTRQFpWARWybIVgQNqqbLmWSur8El2tui5EUwdtIuhBO2tBx5qSXOSVTND7FXrw7ucEIdYHE_QytwU3hVpWXFIuS3aWeyT3bvI2bbBAtOSMiwTRFdLeheChqx-8OaT7p4b1Ymy9GlsnY-vF2HpONW9PwlNzgPax4q-TCXh3AlTQaux88tCEM8eLkgiSJ46tXEgp24M_T_i_7m_Won2Izp9Fcym5SBv9AbxnxX4</recordid><startdate>20111001</startdate><enddate>20111001</enddate><creator>Meuser, Jonathan E.</creator><creator>Boyd, Eric S.</creator><creator>Ananyev, Gennady</creator><creator>Karns, Devin</creator><creator>Radakovits, Randor</creator><creator>Murthy, U. 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M. Narayana</au><au>Ghirardi, Maria L.</au><au>Dismukes, G. Charles</au><au>Peters, John W.</au><au>Posewitz, Matthew C.</au><aucorp>National Renewable Energy Lab. (NREL), Golden, CO (United States)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evolutionary significance of an algal gene encoding an [FeFe]-hydrogenase with F-domain homology and hydrogenase activity in Chlorella variabilis NC64A</atitle><jtitle>Planta</jtitle><stitle>Planta</stitle><addtitle>Planta</addtitle><date>2011-10-01</date><risdate>2011</risdate><volume>234</volume><issue>4</issue><spage>829</spage><epage>843</epage><pages>829-843</pages><issn>0032-0935</issn><eissn>1432-2048</eissn><coden>PLANAB</coden><abstract>[FeFe]-hydrogenases (HYDA) link the production of molecular H2 to anaerobic metabolism in many green algae. Similar to Chlamydomonas reinhardtii, Chlorella variabilis NC64A (Trebouxiophyceae, Chlorophyta) exhibits [FeFe]-hydrogenase (HYDA) activity during anoxia. In contrast to C. reinhardtii and other chlorophycean algae, which contain hydrogenases with only the HYDA active site (H-cluster), C. variabilis NC64A is the only known green alga containing HYDA genes encoding accessory FeS cluster-binding domains (F-cluster). cDNA sequencing confirmed the presence of F-cluster HYDA1 mRNA transcripts, and identified deviations from the in silico splicing models. We show that HYDA activity in C. variabilis NC64A is coupled to anoxic photosynthetic electron transport (PSII linked, as well as PSII-independent) and dark fermentation. We also show that the in vivo H2-photoproduction activity observed is as O2 sensitive as in C. reinhardtii. The two C. variabilis NC64A HYDA sequences are similar to homologs found in more deeply branching bacteria (Thermotogales), diatoms, and heterotrophic flagellates, suggesting that an F-cluster HYDA is the ancestral enzyme in algae. Phylogenetic analysis indicates that the algal HYDA H-cluster domains are monophyletic, suggesting that they share a common origin, and evolved from a single ancestral F-cluster HYDA. Furthermore, phylogenetic reconstruction indicates that the multiple algal HYDA paralogs are the result of gene duplication events that occurred independently within each algal lineage. Collectively, comparative genomic, physiological, and phylogenetic analyses of the C. variabilis NC64A hydrogenase has provided new insights into the molecular evolution and diversity of algal [FeFe]-hydrogenases.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer</pub><pmid>21643991</pmid><doi>10.1007/s00425-011-1431-y</doi><tpages>15</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0032-0935 |
| ispartof | Planta, 2011-10, Vol.234 (4), p.829-843 |
| issn | 0032-0935 1432-2048 |
| language | eng |
| recordid | cdi_osti_scitechconnect_1036398 |
| source | Jstor Complete Legacy; MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Agriculture ALGAE Amino Acid Sequence Anaerobiosis ANOXIA Aquatic plants BACTERIA Base Sequence BASIC BIOLOGICAL SCIENCES Biological and medical sciences Biomedical and Life Sciences Cell Hypoxia CHLAMYDOMONAS Chlamydomonas reinhardtii - enzymology Chlamydomonas reinhardtii - genetics Chlamydomonas reinhardtii - metabolism CHLORELLA Chlorella - enzymology Chlorella - genetics Chlorella - metabolism chlorella variablilis NC64A Chlorophyll - metabolism Complementary DNA Culture Media Darkness DIATOMS DNA, Complementary - genetics DNA, Plant - genetics Ecology ELECTRONS ENZYMES Evolution Evolution, Molecular F-cluster domain FERMENTATION Forestry Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Enzymologic - genetics Gene Expression Regulation, Plant GENES Genomes Genomics Green algae HYDA Hydrogen - metabolism Hydrogenase - genetics Hydrogenase - metabolism HYDROGENASES IN VIVO INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY Iron sulfides Iron-Sulfur Proteins - genetics Iron-Sulfur Proteins - metabolism Life Sciences Light METABOLISM Molecular Sequence Data NAD - metabolism ORIGIN Original Article Oxidation-Reduction Oxygen - metabolism Phylogenetics Phylogeny Plant Proteins - genetics Plant Proteins - metabolism Plant Sciences PRODUCTION Recombinant Proteins RNA, Plant - genetics SPLICING Sugars Time Factors TRANSPORT |
| title | Evolutionary significance of an algal gene encoding an [FeFe]-hydrogenase with F-domain homology and hydrogenase activity in Chlorella variabilis NC64A |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-05T13%3A11%3A49IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_osti_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Evolutionary%20significance%20of%20an%20algal%20gene%20encoding%20an%20%5BFeFe%5D-hydrogenase%20with%20F-domain%20homology%20and%20hydrogenase%20activity%20in%20Chlorella%20variabilis%20NC64A&rft.jtitle=Planta&rft.au=Meuser,%20Jonathan%20E.&rft.aucorp=National%20Renewable%20Energy%20Lab.%20(NREL),%20Golden,%20CO%20(United%20States)&rft.date=2011-10-01&rft.volume=234&rft.issue=4&rft.spage=829&rft.epage=843&rft.pages=829-843&rft.issn=0032-0935&rft.eissn=1432-2048&rft.coden=PLANAB&rft_id=info:doi/10.1007/s00425-011-1431-y&rft_dat=%3Cjstor_osti_%3E23884646%3C/jstor_osti_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=894174246&rft_id=info:pmid/21643991&rft_jstor_id=23884646&rfr_iscdi=true |