The hypE gene completes the gene cluster for H2-oxidation in Azotobacter vinelandii
The nucleotide sequence was obtained for the hypE gene in the cluster of structural and accessory genes required for the assembly and functioning of the membrane-bound, dimeric, (NiFe)hydrogenase in Azotobacter vinelandii. The hypE gene encodes a polypeptide of 341 amino acid residues which is rich...
Gespeichert in:
| Veröffentlicht in: | Journal of molecular biology 1994-02, Vol.236 (1), p.390-396 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 396 |
|---|---|
| container_issue | 1 |
| container_start_page | 390 |
| container_title | Journal of molecular biology |
| container_volume | 236 |
| creator | GARG, R. P MENON, A. L JACOBS, K ROBSON, R. M ROBSON, R. L |
| description | The nucleotide sequence was obtained for the hypE gene in the cluster of structural and accessory genes required for the assembly and functioning of the membrane-bound, dimeric, (NiFe)hydrogenase in Azotobacter vinelandii. The hypE gene encodes a polypeptide of 341 amino acid residues which is rich in alanine, glycine, valine and proline and appears to be involved in maturation of the enzyme because chromosomal mutations in hypE block O2-dependent H2-oxidation and affect the amount, processing and localization of the (NiFe) hydrogenase alpha-subunit. The complete nucleotide sequence for the hydrogenase gene cluster in A. vinelandii has now been assembled into a contiguous sequence of 13,914 bp containing 16 potential genes which appear to be transcribed undirectionally. They are arranged in the order hoxK, hoxG, hoxZ, hoxM, hoxL, hoxO, hoxQ, hoxR, hoxT, hoxV, hypA, hypB, hypF, hypC, hypD and hypE. This cluster closely resembles those described for comparable (NiFe) hydrogenases in other bacteria. |
| doi_str_mv | 10.1006/jmbi.1994.1149 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_76360933</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>76360933</sourcerecordid><originalsourceid>FETCH-LOGICAL-c234t-b5962dc25d3db80cdd34039d9b74f81980d9d5cddfe7ccd19a45bb9d4ddab3353</originalsourceid><addsrcrecordid>eNo9kEtLw0AURgdRaq1u3QmzEHeJ88pjlqVUKxRcWNfDvGKnJJmYScT6601o6OrC9517uRwA7jGKMULp86FSLsacsxhjxi_AHKOcR3lK80swR4iQiOQ0vQY3IRwQQgll-QzMMo5SitEcfOz2Fu6PzRp-2dpC7aumtJ0NsBvyU1T2obMtLHwLNyTyv87Izvkauhou_3znldRj_-NqW8raOHcLrgpZBns3zQX4fFnvVpto-_76tlpuI00o6yKV8JQYTRJDjcqRNoYyRLnhKmNFjnmODDfJEBc209pgLlmiFDfMGKkoTegCPJ3uNq3_7m3oROWCtuXwhfV9EFlKU8QpHcD4BOrWh9DaQjStq2R7FBiJ0aIYLYrRohgtDgsP0-VeVdac8Unb0D9OvQxalkUra-3CGaOcJCTl9B_4CHuP</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>76360933</pqid></control><display><type>article</type><title>The hypE gene completes the gene cluster for H2-oxidation in Azotobacter vinelandii</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>GARG, R. P ; MENON, A. L ; JACOBS, K ; ROBSON, R. M ; ROBSON, R. L</creator><creatorcontrib>GARG, R. P ; MENON, A. L ; JACOBS, K ; ROBSON, R. M ; ROBSON, R. L</creatorcontrib><description>The nucleotide sequence was obtained for the hypE gene in the cluster of structural and accessory genes required for the assembly and functioning of the membrane-bound, dimeric, (NiFe)hydrogenase in Azotobacter vinelandii. The hypE gene encodes a polypeptide of 341 amino acid residues which is rich in alanine, glycine, valine and proline and appears to be involved in maturation of the enzyme because chromosomal mutations in hypE block O2-dependent H2-oxidation and affect the amount, processing and localization of the (NiFe) hydrogenase alpha-subunit. The complete nucleotide sequence for the hydrogenase gene cluster in A. vinelandii has now been assembled into a contiguous sequence of 13,914 bp containing 16 potential genes which appear to be transcribed undirectionally. They are arranged in the order hoxK, hoxG, hoxZ, hoxM, hoxL, hoxO, hoxQ, hoxR, hoxT, hoxV, hypA, hypB, hypF, hypC, hypD and hypE. This cluster closely resembles those described for comparable (NiFe) hydrogenases in other bacteria.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1006/jmbi.1994.1149</identifier><identifier>PMID: 7906310</identifier><identifier>CODEN: JMOBAK</identifier><language>eng</language><publisher>Oxford: Elsevier</publisher><subject>Amino Acid Sequence ; Azotobacter vinelandii - enzymology ; Azotobacter vinelandii - genetics ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Base Sequence ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Genes, Bacterial ; Genes, Homeobox ; Genes. Genome ; Hydrogenase - genetics ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Multigene Family ; Restriction Mapping ; Sequence Homology, Amino Acid</subject><ispartof>Journal of molecular biology, 1994-02, Vol.236 (1), p.390-396</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c234t-b5962dc25d3db80cdd34039d9b74f81980d9d5cddfe7ccd19a45bb9d4ddab3353</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3925269$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7906310$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>GARG, R. P</creatorcontrib><creatorcontrib>MENON, A. L</creatorcontrib><creatorcontrib>JACOBS, K</creatorcontrib><creatorcontrib>ROBSON, R. M</creatorcontrib><creatorcontrib>ROBSON, R. L</creatorcontrib><title>The hypE gene completes the gene cluster for H2-oxidation in Azotobacter vinelandii</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>The nucleotide sequence was obtained for the hypE gene in the cluster of structural and accessory genes required for the assembly and functioning of the membrane-bound, dimeric, (NiFe)hydrogenase in Azotobacter vinelandii. The hypE gene encodes a polypeptide of 341 amino acid residues which is rich in alanine, glycine, valine and proline and appears to be involved in maturation of the enzyme because chromosomal mutations in hypE block O2-dependent H2-oxidation and affect the amount, processing and localization of the (NiFe) hydrogenase alpha-subunit. The complete nucleotide sequence for the hydrogenase gene cluster in A. vinelandii has now been assembled into a contiguous sequence of 13,914 bp containing 16 potential genes which appear to be transcribed undirectionally. They are arranged in the order hoxK, hoxG, hoxZ, hoxM, hoxL, hoxO, hoxQ, hoxR, hoxT, hoxV, hypA, hypB, hypF, hypC, hypD and hypE. This cluster closely resembles those described for comparable (NiFe) hydrogenases in other bacteria.</description><subject>Amino Acid Sequence</subject><subject>Azotobacter vinelandii - enzymology</subject><subject>Azotobacter vinelandii - genetics</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Bacterial</subject><subject>Genes, Homeobox</subject><subject>Genes. Genome</subject><subject>Hydrogenase - genetics</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Multigene Family</subject><subject>Restriction Mapping</subject><subject>Sequence Homology, Amino Acid</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEtLw0AURgdRaq1u3QmzEHeJ88pjlqVUKxRcWNfDvGKnJJmYScT6601o6OrC9517uRwA7jGKMULp86FSLsacsxhjxi_AHKOcR3lK80swR4iQiOQ0vQY3IRwQQgll-QzMMo5SitEcfOz2Fu6PzRp-2dpC7aumtJ0NsBvyU1T2obMtLHwLNyTyv87Izvkauhou_3znldRj_-NqW8raOHcLrgpZBns3zQX4fFnvVpto-_76tlpuI00o6yKV8JQYTRJDjcqRNoYyRLnhKmNFjnmODDfJEBc209pgLlmiFDfMGKkoTegCPJ3uNq3_7m3oROWCtuXwhfV9EFlKU8QpHcD4BOrWh9DaQjStq2R7FBiJ0aIYLYrRohgtDgsP0-VeVdac8Unb0D9OvQxalkUra-3CGaOcJCTl9B_4CHuP</recordid><startdate>19940211</startdate><enddate>19940211</enddate><creator>GARG, R. P</creator><creator>MENON, A. L</creator><creator>JACOBS, K</creator><creator>ROBSON, R. M</creator><creator>ROBSON, R. L</creator><general>Elsevier</general><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>7X8</scope></search><sort><creationdate>19940211</creationdate><title>The hypE gene completes the gene cluster for H2-oxidation in Azotobacter vinelandii</title><author>GARG, R. P ; MENON, A. L ; JACOBS, K ; ROBSON, R. M ; ROBSON, R. L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c234t-b5962dc25d3db80cdd34039d9b74f81980d9d5cddfe7ccd19a45bb9d4ddab3353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Azotobacter vinelandii - enzymology</topic><topic>Azotobacter vinelandii - genetics</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Bacterial</topic><topic>Genes, Homeobox</topic><topic>Genes. Genome</topic><topic>Hydrogenase - genetics</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Multigene Family</topic><topic>Restriction Mapping</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>GARG, R. P</creatorcontrib><creatorcontrib>MENON, A. L</creatorcontrib><creatorcontrib>JACOBS, K</creatorcontrib><creatorcontrib>ROBSON, R. M</creatorcontrib><creatorcontrib>ROBSON, R. L</creatorcontrib><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>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>GARG, R. P</au><au>MENON, A. L</au><au>JACOBS, K</au><au>ROBSON, R. M</au><au>ROBSON, R. L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The hypE gene completes the gene cluster for H2-oxidation in Azotobacter vinelandii</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1994-02-11</date><risdate>1994</risdate><volume>236</volume><issue>1</issue><spage>390</spage><epage>396</epage><pages>390-396</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><coden>JMOBAK</coden><abstract>The nucleotide sequence was obtained for the hypE gene in the cluster of structural and accessory genes required for the assembly and functioning of the membrane-bound, dimeric, (NiFe)hydrogenase in Azotobacter vinelandii. The hypE gene encodes a polypeptide of 341 amino acid residues which is rich in alanine, glycine, valine and proline and appears to be involved in maturation of the enzyme because chromosomal mutations in hypE block O2-dependent H2-oxidation and affect the amount, processing and localization of the (NiFe) hydrogenase alpha-subunit. The complete nucleotide sequence for the hydrogenase gene cluster in A. vinelandii has now been assembled into a contiguous sequence of 13,914 bp containing 16 potential genes which appear to be transcribed undirectionally. They are arranged in the order hoxK, hoxG, hoxZ, hoxM, hoxL, hoxO, hoxQ, hoxR, hoxT, hoxV, hypA, hypB, hypF, hypC, hypD and hypE. This cluster closely resembles those described for comparable (NiFe) hydrogenases in other bacteria.</abstract><cop>Oxford</cop><pub>Elsevier</pub><pmid>7906310</pmid><doi>10.1006/jmbi.1994.1149</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-2836 |
| ispartof | Journal of molecular biology, 1994-02, Vol.236 (1), p.390-396 |
| issn | 0022-2836 1089-8638 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76360933 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence Azotobacter vinelandii - enzymology Azotobacter vinelandii - genetics Bacterial Proteins - chemistry Bacterial Proteins - genetics Base Sequence Biological and medical sciences Fundamental and applied biological sciences. Psychology Genes, Bacterial Genes, Homeobox Genes. Genome Hydrogenase - genetics Molecular and cellular biology Molecular genetics Molecular Sequence Data Multigene Family Restriction Mapping Sequence Homology, Amino Acid |
| title | The hypE gene completes the gene cluster for H2-oxidation in Azotobacter vinelandii |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-22T13%3A26%3A18IST&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=The%20hypE%20gene%20completes%20the%20gene%20cluster%20for%20H2-oxidation%20in%20Azotobacter%20vinelandii&rft.jtitle=Journal%20of%20molecular%20biology&rft.au=GARG,%20R.%20P&rft.date=1994-02-11&rft.volume=236&rft.issue=1&rft.spage=390&rft.epage=396&rft.pages=390-396&rft.issn=0022-2836&rft.eissn=1089-8638&rft.coden=JMOBAK&rft_id=info:doi/10.1006/jmbi.1994.1149&rft_dat=%3Cproquest_cross%3E76360933%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=76360933&rft_id=info:pmid/7906310&rfr_iscdi=true |