High diversity and complex evolution of fungal cytochrome P450 reductase: Cytochrome P450 systems
Cytochrome P450 reductase (CPR) is the redox partner of P450 monooxygenases, involved in primary and secondary metabolism of eukaryotes. Two novel CPR genes, sharing 34% amino acid identity, were found in the filamentous ascomycete Cochliobolus lunatus. Fungal genomes were searched for putative CPR...
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| Veröffentlicht in: | Fungal genetics and biology 2008-04, Vol.45 (4), p.446-458 |
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| creator | Lah, Ljerka Kraševec, Nada Trontelj, Peter Komel, Radovan |
| description | Cytochrome P450 reductase (CPR) is the redox partner of P450 monooxygenases, involved in primary and secondary metabolism of eukaryotes. Two novel CPR genes, sharing 34% amino acid identity, were found in the filamentous ascomycete
Cochliobolus lunatus. Fungal genomes were searched for putative CPR enzymes. Phylogenetic analysis suggests that multiple independent CPR duplication events occurred in fungi, whereas P450–CPR fusion occurred before the diversification of Dikarya and Zygomycota. Additionally, losses of methionine synthase reductase were found in certain fungal taxa; a truncated form of this enzyme was conserved in Pezizomycotina. In fungi, high numbers of cytochrome P450 enzymes, multiple CPRs, and P450–CPR fusion proteins were associated with filamentous growth. Evolution of multiple CPR-like oxidoreductases in filamentous fungi might have been driven by the complexity of biochemical functions necessitated by their growth form, as opposed to yeast. |
| doi_str_mv | 10.1016/j.fgb.2007.10.004 |
| format | Article |
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Cochliobolus lunatus. Fungal genomes were searched for putative CPR enzymes. Phylogenetic analysis suggests that multiple independent CPR duplication events occurred in fungi, whereas P450–CPR fusion occurred before the diversification of Dikarya and Zygomycota. Additionally, losses of methionine synthase reductase were found in certain fungal taxa; a truncated form of this enzyme was conserved in Pezizomycotina. In fungi, high numbers of cytochrome P450 enzymes, multiple CPRs, and P450–CPR fusion proteins were associated with filamentous growth. Evolution of multiple CPR-like oxidoreductases in filamentous fungi might have been driven by the complexity of biochemical functions necessitated by their growth form, as opposed to yeast.</description><identifier>ISSN: 1087-1845</identifier><identifier>EISSN: 1096-0937</identifier><identifier>DOI: 10.1016/j.fgb.2007.10.004</identifier><identifier>PMID: 18024101</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>amino acid sequences ; Ascomycetes ; Ascomycota - enzymology ; Ascomycota - genetics ; Bayesian inference ; Cochliobolus lunatus ; CPR ; cytochrome P-450 ; Cytochrome P-450 Enzyme System - genetics ; DNA, Fungal - chemistry ; DNA, Fungal - genetics ; enzyme activity ; evolution ; Evolution, Molecular ; Ferredoxin-NADP Reductase - genetics ; Fungal Proteins - genetics ; Fungi ; Gene Deletion ; Gene Duplication ; Gene Fusion ; Genetic Variation ; genome ; genomics ; methionine synthase reductase ; Molecular Sequence Data ; MSR ; NADPH-Ferrihemoprotein Reductase - genetics ; NR1 ; nucleotide sequences ; oxidoreductases ; oxygenases ; Phylogeny ; Protein evolution ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Zygomycota</subject><ispartof>Fungal genetics and biology, 2008-04, Vol.45 (4), p.446-458</ispartof><rights>2007 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c406t-534b6c49611d43b025ed8edcbf643ecc14b0426a7aea4f8555f1228a63255cb13</citedby><cites>FETCH-LOGICAL-c406t-534b6c49611d43b025ed8edcbf643ecc14b0426a7aea4f8555f1228a63255cb13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.fgb.2007.10.004$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18024101$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lah, Ljerka</creatorcontrib><creatorcontrib>Kraševec, Nada</creatorcontrib><creatorcontrib>Trontelj, Peter</creatorcontrib><creatorcontrib>Komel, Radovan</creatorcontrib><title>High diversity and complex evolution of fungal cytochrome P450 reductase: Cytochrome P450 systems</title><title>Fungal genetics and biology</title><addtitle>Fungal Genet Biol</addtitle><description>Cytochrome P450 reductase (CPR) is the redox partner of P450 monooxygenases, involved in primary and secondary metabolism of eukaryotes. Two novel CPR genes, sharing 34% amino acid identity, were found in the filamentous ascomycete
Cochliobolus lunatus. Fungal genomes were searched for putative CPR enzymes. Phylogenetic analysis suggests that multiple independent CPR duplication events occurred in fungi, whereas P450–CPR fusion occurred before the diversification of Dikarya and Zygomycota. Additionally, losses of methionine synthase reductase were found in certain fungal taxa; a truncated form of this enzyme was conserved in Pezizomycotina. In fungi, high numbers of cytochrome P450 enzymes, multiple CPRs, and P450–CPR fusion proteins were associated with filamentous growth. Evolution of multiple CPR-like oxidoreductases in filamentous fungi might have been driven by the complexity of biochemical functions necessitated by their growth form, as opposed to yeast.</description><subject>amino acid sequences</subject><subject>Ascomycetes</subject><subject>Ascomycota - enzymology</subject><subject>Ascomycota - genetics</subject><subject>Bayesian inference</subject><subject>Cochliobolus lunatus</subject><subject>CPR</subject><subject>cytochrome P-450</subject><subject>Cytochrome P-450 Enzyme System - genetics</subject><subject>DNA, Fungal - chemistry</subject><subject>DNA, Fungal - genetics</subject><subject>enzyme activity</subject><subject>evolution</subject><subject>Evolution, Molecular</subject><subject>Ferredoxin-NADP Reductase - genetics</subject><subject>Fungal Proteins - genetics</subject><subject>Fungi</subject><subject>Gene Deletion</subject><subject>Gene Duplication</subject><subject>Gene Fusion</subject><subject>Genetic Variation</subject><subject>genome</subject><subject>genomics</subject><subject>methionine synthase reductase</subject><subject>Molecular Sequence Data</subject><subject>MSR</subject><subject>NADPH-Ferrihemoprotein Reductase - genetics</subject><subject>NR1</subject><subject>nucleotide sequences</subject><subject>oxidoreductases</subject><subject>oxygenases</subject><subject>Phylogeny</subject><subject>Protein evolution</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>Zygomycota</subject><issn>1087-1845</issn><issn>1096-0937</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUGP0zAQhS0EYpeFH8AFfOKWMnZsJ4ETqoBFWgkk2LPl2OOuqyQudlLRf4-jVkLiAKfxeL55Gr1HyEsGGwZMvd1v_K7fcICm9BsA8YhcM-hUBV3dPF7fbVOxVsgr8iznPQBjUrCn5Iq1wEWRuCbmNuweqAtHTDnMJ2omR20cDwP-oniMwzKHONHoqV-mnRmoPc3RPqQ4Iv0mJNCEbrGzyfiObv8a5VOecczPyRNvhowvLvWG3H_6-GN7W919_fxl--GusgLUXMla9MqKTjHmRN0Dl-hadLb3StRoLRM9CK5MY9AI30opPeO8NarmUtqe1TfkzVn3kOLPBfOsx5AtDoOZMC5ZN1CLjrfivyAHJVWrVpCdQZtizgm9PqQwmnTSDPQagN7rEoBeA1i_SgBl59VFfOlHdH82Lo4X4PUZ8CZqs0sh6_vvvAwAOihOrMT7M4HFrWPApLMNOFl0IaGdtYvhHwf8BjqJnnY</recordid><startdate>20080401</startdate><enddate>20080401</enddate><creator>Lah, Ljerka</creator><creator>Kraševec, Nada</creator><creator>Trontelj, Peter</creator><creator>Komel, Radovan</creator><general>Elsevier Inc</general><scope>FBQ</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>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20080401</creationdate><title>High diversity and complex evolution of fungal cytochrome P450 reductase: Cytochrome P450 systems</title><author>Lah, Ljerka ; Kraševec, Nada ; Trontelj, Peter ; Komel, Radovan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c406t-534b6c49611d43b025ed8edcbf643ecc14b0426a7aea4f8555f1228a63255cb13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>amino acid sequences</topic><topic>Ascomycetes</topic><topic>Ascomycota - enzymology</topic><topic>Ascomycota - genetics</topic><topic>Bayesian inference</topic><topic>Cochliobolus lunatus</topic><topic>CPR</topic><topic>cytochrome P-450</topic><topic>Cytochrome P-450 Enzyme System - genetics</topic><topic>DNA, Fungal - chemistry</topic><topic>DNA, Fungal - genetics</topic><topic>enzyme activity</topic><topic>evolution</topic><topic>Evolution, Molecular</topic><topic>Ferredoxin-NADP Reductase - genetics</topic><topic>Fungal Proteins - genetics</topic><topic>Fungi</topic><topic>Gene Deletion</topic><topic>Gene Duplication</topic><topic>Gene Fusion</topic><topic>Genetic Variation</topic><topic>genome</topic><topic>genomics</topic><topic>methionine synthase reductase</topic><topic>Molecular Sequence Data</topic><topic>MSR</topic><topic>NADPH-Ferrihemoprotein Reductase - genetics</topic><topic>NR1</topic><topic>nucleotide sequences</topic><topic>oxidoreductases</topic><topic>oxygenases</topic><topic>Phylogeny</topic><topic>Protein evolution</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>Zygomycota</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lah, Ljerka</creatorcontrib><creatorcontrib>Kraševec, Nada</creatorcontrib><creatorcontrib>Trontelj, Peter</creatorcontrib><creatorcontrib>Komel, Radovan</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Fungal genetics and biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lah, Ljerka</au><au>Kraševec, Nada</au><au>Trontelj, Peter</au><au>Komel, Radovan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>High diversity and complex evolution of fungal cytochrome P450 reductase: Cytochrome P450 systems</atitle><jtitle>Fungal genetics and biology</jtitle><addtitle>Fungal Genet Biol</addtitle><date>2008-04-01</date><risdate>2008</risdate><volume>45</volume><issue>4</issue><spage>446</spage><epage>458</epage><pages>446-458</pages><issn>1087-1845</issn><eissn>1096-0937</eissn><abstract>Cytochrome P450 reductase (CPR) is the redox partner of P450 monooxygenases, involved in primary and secondary metabolism of eukaryotes. Two novel CPR genes, sharing 34% amino acid identity, were found in the filamentous ascomycete
Cochliobolus lunatus. Fungal genomes were searched for putative CPR enzymes. Phylogenetic analysis suggests that multiple independent CPR duplication events occurred in fungi, whereas P450–CPR fusion occurred before the diversification of Dikarya and Zygomycota. Additionally, losses of methionine synthase reductase were found in certain fungal taxa; a truncated form of this enzyme was conserved in Pezizomycotina. In fungi, high numbers of cytochrome P450 enzymes, multiple CPRs, and P450–CPR fusion proteins were associated with filamentous growth. Evolution of multiple CPR-like oxidoreductases in filamentous fungi might have been driven by the complexity of biochemical functions necessitated by their growth form, as opposed to yeast.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18024101</pmid><doi>10.1016/j.fgb.2007.10.004</doi><tpages>13</tpages></addata></record> |
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| subjects | amino acid sequences Ascomycetes Ascomycota - enzymology Ascomycota - genetics Bayesian inference Cochliobolus lunatus CPR cytochrome P-450 Cytochrome P-450 Enzyme System - genetics DNA, Fungal - chemistry DNA, Fungal - genetics enzyme activity evolution Evolution, Molecular Ferredoxin-NADP Reductase - genetics Fungal Proteins - genetics Fungi Gene Deletion Gene Duplication Gene Fusion Genetic Variation genome genomics methionine synthase reductase Molecular Sequence Data MSR NADPH-Ferrihemoprotein Reductase - genetics NR1 nucleotide sequences oxidoreductases oxygenases Phylogeny Protein evolution Sequence Analysis, DNA Sequence Homology, Amino Acid Zygomycota |
| title | High diversity and complex evolution of fungal cytochrome P450 reductase: Cytochrome P450 systems |
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