Loading…

Divergent evolution of chloroplast-type ferredoxins

The TOL plasmid PWWO of Pseudomonas putida encodes a set of enzymes required for the oxidation of toluene to Krebs cycle intermediates. The structural genes for these enzymes are encoded in two operons which comprise the xylCMABN and xylXYZLTEGFJQKIH genes, respectively. The function of the xylT gen...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 1991-07, Vol.285 (1), p.85-88
Main Authors: Harayama, Shigeaki, Polissi, Alessandra, Rekik, Monique
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c481Q-333f55ed0a3f126cd0bca58d99a57477c6e14ce434551f338a61bd44c17a8bb3
cites cdi_FETCH-LOGICAL-c481Q-333f55ed0a3f126cd0bca58d99a57477c6e14ce434551f338a61bd44c17a8bb3
container_end_page 88
container_issue 1
container_start_page 85
container_title FEBS letters
container_volume 285
creator Harayama, Shigeaki
Polissi, Alessandra
Rekik, Monique
description The TOL plasmid PWWO of Pseudomonas putida encodes a set of enzymes required for the oxidation of toluene to Krebs cycle intermediates. The structural genes for these enzymes are encoded in two operons which comprise the xylCMABN and xylXYZLTEGFJQKIH genes, respectively. The function of the xylT gene has not yet been identified. The nucleotide sequence of xylT was determined in this study and putative gene product was shown to contain a sequence characteristic for chloroplast-type ferredoxins. The nahT gene, the homologue of xylT, present on NAH plasmid NAH7 encoding naphtalene-degrading enzymes, was also sequenced. The sequence conservation between xylT and nahT strongly suggests that both gene products have some physiological function. Chloroplast-type ferredoxins have been discovered in photosynthetic organisms (plants, algae, cyanobacteria and Rhodobacter) and Halobacterium species. Furthermore, chloroplast-type ferredoxin-like sequences have been found in the electron-transfer components of some oxygenases, The sequences of XylT and NahT were compared with those of the previously identified chloroplast-type ferredoxins, in order to examine their evolutionary relationships.
doi_str_mv 10.1016/0014-5793(91)80730-Q
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80662665</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>001457939180730Q</els_id><sourcerecordid>80662665</sourcerecordid><originalsourceid>FETCH-LOGICAL-c481Q-333f55ed0a3f126cd0bca58d99a57477c6e14ce434551f338a61bd44c17a8bb3</originalsourceid><addsrcrecordid>eNqNkE1PGzEQhq0KRFPaf9BKuYDgsNSz_r4gUUoKElIVibvl9c6Cq806tTeh-ffskghuhZPlmWfesR9CvgI9AwryO6XAC6EMOzFwqqlitJh_IBPQihWMS71HJi_IR_Ip5z90uGswB-SgpFIoLSaE_QxrTPfY9VNcx3bVh9hNYzP1D21Mcdm63Bf9ZonTBlPCOv4LXf5M9hvXZvyyOw_J3ezq7vK6uP396-by4rbwXMO8YIw1QmBNHWuglL6mlXdC18Y4obhSXiJwj5xxIaBhTDsJVc25B-V0VbFDcryNXab4d4W5t4uQPbat6zCustVUylJK8SYIkpal0XwA-Rb0KeacsLHLFBYubSxQOzq1ozA7CrMG7LNTOx_Gvu3yV9UC65ehncShf7Tru-xd2yTX-ZBfs41SgrGRm225x9Di5l277ezqRzk2xrqB5-r4oPNtEA721wGTzT5g57EOCX1v6xj-_6Mn68ylog</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16022984</pqid></control><display><type>article</type><title>Divergent evolution of chloroplast-type ferredoxins</title><source>Elsevier ScienceDirect Journals</source><creator>Harayama, Shigeaki ; Polissi, Alessandra ; Rekik, Monique</creator><creatorcontrib>Harayama, Shigeaki ; Polissi, Alessandra ; Rekik, Monique</creatorcontrib><description>The TOL plasmid PWWO of Pseudomonas putida encodes a set of enzymes required for the oxidation of toluene to Krebs cycle intermediates. The structural genes for these enzymes are encoded in two operons which comprise the xylCMABN and xylXYZLTEGFJQKIH genes, respectively. The function of the xylT gene has not yet been identified. The nucleotide sequence of xylT was determined in this study and putative gene product was shown to contain a sequence characteristic for chloroplast-type ferredoxins. The nahT gene, the homologue of xylT, present on NAH plasmid NAH7 encoding naphtalene-degrading enzymes, was also sequenced. The sequence conservation between xylT and nahT strongly suggests that both gene products have some physiological function. Chloroplast-type ferredoxins have been discovered in photosynthetic organisms (plants, algae, cyanobacteria and Rhodobacter) and Halobacterium species. Furthermore, chloroplast-type ferredoxin-like sequences have been found in the electron-transfer components of some oxygenases, The sequences of XylT and NahT were compared with those of the previously identified chloroplast-type ferredoxins, in order to examine their evolutionary relationships.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(91)80730-Q</identifier><identifier>PMID: 2065785</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Bacterial Proteins ; Base Sequence ; Biological and medical sciences ; Biological Evolution ; Chloroplast-type ; Chloroplasts ; Ferredoxin ; Ferredoxins - chemistry ; Ferredoxins - genetics ; Fundamental and applied biological sciences. Psychology ; Gene Frequency ; Genetics of eukaryotes. Biological and molecular evolution ; Molecular Sequence Data ; NAH plasmid ; Naphthalenes - metabolism ; Plasmids - genetics ; Protein evolution ; Pseudomonas - genetics ; Pseudomonas putida ; Sequence Alignment ; Sequence Homology, Nucleic Acid ; TOL plasmid ; Toluene - metabolism</subject><ispartof>FEBS letters, 1991-07, Vol.285 (1), p.85-88</ispartof><rights>1991</rights><rights>FEBS Letters 285 (1991) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c481Q-333f55ed0a3f126cd0bca58d99a57477c6e14ce434551f338a61bd44c17a8bb3</citedby><cites>FETCH-LOGICAL-c481Q-333f55ed0a3f126cd0bca58d99a57477c6e14ce434551f338a61bd44c17a8bb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/001457939180730Q$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27924,27925,45780</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=19775335$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2065785$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Harayama, Shigeaki</creatorcontrib><creatorcontrib>Polissi, Alessandra</creatorcontrib><creatorcontrib>Rekik, Monique</creatorcontrib><title>Divergent evolution of chloroplast-type ferredoxins</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The TOL plasmid PWWO of Pseudomonas putida encodes a set of enzymes required for the oxidation of toluene to Krebs cycle intermediates. The structural genes for these enzymes are encoded in two operons which comprise the xylCMABN and xylXYZLTEGFJQKIH genes, respectively. The function of the xylT gene has not yet been identified. The nucleotide sequence of xylT was determined in this study and putative gene product was shown to contain a sequence characteristic for chloroplast-type ferredoxins. The nahT gene, the homologue of xylT, present on NAH plasmid NAH7 encoding naphtalene-degrading enzymes, was also sequenced. The sequence conservation between xylT and nahT strongly suggests that both gene products have some physiological function. Chloroplast-type ferredoxins have been discovered in photosynthetic organisms (plants, algae, cyanobacteria and Rhodobacter) and Halobacterium species. Furthermore, chloroplast-type ferredoxin-like sequences have been found in the electron-transfer components of some oxygenases, The sequences of XylT and NahT were compared with those of the previously identified chloroplast-type ferredoxins, in order to examine their evolutionary relationships.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biological Evolution</subject><subject>Chloroplast-type</subject><subject>Chloroplasts</subject><subject>Ferredoxin</subject><subject>Ferredoxins - chemistry</subject><subject>Ferredoxins - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Frequency</subject><subject>Genetics of eukaryotes. Biological and molecular evolution</subject><subject>Molecular Sequence Data</subject><subject>NAH plasmid</subject><subject>Naphthalenes - metabolism</subject><subject>Plasmids - genetics</subject><subject>Protein evolution</subject><subject>Pseudomonas - genetics</subject><subject>Pseudomonas putida</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>TOL plasmid</subject><subject>Toluene - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><recordid>eNqNkE1PGzEQhq0KRFPaf9BKuYDgsNSz_r4gUUoKElIVibvl9c6Cq806tTeh-ffskghuhZPlmWfesR9CvgI9AwryO6XAC6EMOzFwqqlitJh_IBPQihWMS71HJi_IR_Ip5z90uGswB-SgpFIoLSaE_QxrTPfY9VNcx3bVh9hNYzP1D21Mcdm63Bf9ZonTBlPCOv4LXf5M9hvXZvyyOw_J3ezq7vK6uP396-by4rbwXMO8YIw1QmBNHWuglL6mlXdC18Y4obhSXiJwj5xxIaBhTDsJVc25B-V0VbFDcryNXab4d4W5t4uQPbat6zCustVUylJK8SYIkpal0XwA-Rb0KeacsLHLFBYubSxQOzq1ozA7CrMG7LNTOx_Gvu3yV9UC65ehncShf7Tru-xd2yTX-ZBfs41SgrGRm225x9Di5l277ezqRzk2xrqB5-r4oPNtEA721wGTzT5g57EOCX1v6xj-_6Mn68ylog</recordid><startdate>19910708</startdate><enddate>19910708</enddate><creator>Harayama, Shigeaki</creator><creator>Polissi, Alessandra</creator><creator>Rekik, Monique</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</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>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19910708</creationdate><title>Divergent evolution of chloroplast-type ferredoxins</title><author>Harayama, Shigeaki ; Polissi, Alessandra ; Rekik, Monique</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c481Q-333f55ed0a3f126cd0bca58d99a57477c6e14ce434551f338a61bd44c17a8bb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biological Evolution</topic><topic>Chloroplast-type</topic><topic>Chloroplasts</topic><topic>Ferredoxin</topic><topic>Ferredoxins - chemistry</topic><topic>Ferredoxins - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Frequency</topic><topic>Genetics of eukaryotes. Biological and molecular evolution</topic><topic>Molecular Sequence Data</topic><topic>NAH plasmid</topic><topic>Naphthalenes - metabolism</topic><topic>Plasmids - genetics</topic><topic>Protein evolution</topic><topic>Pseudomonas - genetics</topic><topic>Pseudomonas putida</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>TOL plasmid</topic><topic>Toluene - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Harayama, Shigeaki</creatorcontrib><creatorcontrib>Polissi, Alessandra</creatorcontrib><creatorcontrib>Rekik, Monique</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Harayama, Shigeaki</au><au>Polissi, Alessandra</au><au>Rekik, Monique</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Divergent evolution of chloroplast-type ferredoxins</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1991-07-08</date><risdate>1991</risdate><volume>285</volume><issue>1</issue><spage>85</spage><epage>88</epage><pages>85-88</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>The TOL plasmid PWWO of Pseudomonas putida encodes a set of enzymes required for the oxidation of toluene to Krebs cycle intermediates. The structural genes for these enzymes are encoded in two operons which comprise the xylCMABN and xylXYZLTEGFJQKIH genes, respectively. The function of the xylT gene has not yet been identified. The nucleotide sequence of xylT was determined in this study and putative gene product was shown to contain a sequence characteristic for chloroplast-type ferredoxins. The nahT gene, the homologue of xylT, present on NAH plasmid NAH7 encoding naphtalene-degrading enzymes, was also sequenced. The sequence conservation between xylT and nahT strongly suggests that both gene products have some physiological function. Chloroplast-type ferredoxins have been discovered in photosynthetic organisms (plants, algae, cyanobacteria and Rhodobacter) and Halobacterium species. Furthermore, chloroplast-type ferredoxin-like sequences have been found in the electron-transfer components of some oxygenases, The sequences of XylT and NahT were compared with those of the previously identified chloroplast-type ferredoxins, in order to examine their evolutionary relationships.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>2065785</pmid><doi>10.1016/0014-5793(91)80730-Q</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0014-5793
ispartof FEBS letters, 1991-07, Vol.285 (1), p.85-88
issn 0014-5793
1873-3468
language eng
recordid cdi_proquest_miscellaneous_80662665
source Elsevier ScienceDirect Journals
subjects Amino Acid Sequence
Bacterial Proteins
Base Sequence
Biological and medical sciences
Biological Evolution
Chloroplast-type
Chloroplasts
Ferredoxin
Ferredoxins - chemistry
Ferredoxins - genetics
Fundamental and applied biological sciences. Psychology
Gene Frequency
Genetics of eukaryotes. Biological and molecular evolution
Molecular Sequence Data
NAH plasmid
Naphthalenes - metabolism
Plasmids - genetics
Protein evolution
Pseudomonas - genetics
Pseudomonas putida
Sequence Alignment
Sequence Homology, Nucleic Acid
TOL plasmid
Toluene - metabolism
title Divergent evolution of chloroplast-type ferredoxins
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T00%3A55%3A45IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Divergent%20evolution%20of%20chloroplast-type%20ferredoxins&rft.jtitle=FEBS%20letters&rft.au=Harayama,%20Shigeaki&rft.date=1991-07-08&rft.volume=285&rft.issue=1&rft.spage=85&rft.epage=88&rft.pages=85-88&rft.issn=0014-5793&rft.eissn=1873-3468&rft.coden=FEBLAL&rft_id=info:doi/10.1016/0014-5793(91)80730-Q&rft_dat=%3Cproquest_cross%3E80662665%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c481Q-333f55ed0a3f126cd0bca58d99a57477c6e14ce434551f338a61bd44c17a8bb3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=16022984&rft_id=info:pmid/2065785&rfr_iscdi=true