Translation termination in pyrrolysine-utilizing archaea
Although some data link archaeal and eukaryotic translation, the overall mechanism of protein synthesis in archaea remains largely obscure. Both archaeal (aRF1) and eukaryotic (eRF1) single release factors recognize all three stop codons. The archaeal genus Methanosarcinaceae contains two aRF1 homol...
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| Veröffentlicht in: | FEBS letters 2009-11, Vol.583 (21), p.3455-3460 |
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| creator | Alkalaeva, Elena Eliseev, Boris Ambrogelly, Alexandre Vlasov, Peter Kondrashov, Fyodor A. Gundllapalli, Sharath Frolova, Lyudmila Söll, Dieter Kisselev, Lev |
| description | Although some data link archaeal and eukaryotic translation, the overall mechanism of protein synthesis in archaea remains largely obscure. Both archaeal (aRF1) and eukaryotic (eRF1) single release factors recognize all three stop codons. The archaeal genus
Methanosarcinaceae contains two aRF1 homologs, and also uses the UAG stop to encode the 22nd amino acid, pyrrolysine. Here we provide an analysis of the last stage of archaeal translation in pyrrolysine-utilizing species. We demonstrated that only one of two
Methanosarcina barkeri aRF1 homologs possesses activity and recognizes all three stop codons. The second aRF1 homolog may have another unknown function. The mechanism of pyrrolysine incorporation in the
Methanosarcinaceae is discussed. |
| doi_str_mv | 10.1016/j.febslet.2009.09.044 |
| format | Article |
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Methanosarcinaceae contains two aRF1 homologs, and also uses the UAG stop to encode the 22nd amino acid, pyrrolysine. Here we provide an analysis of the last stage of archaeal translation in pyrrolysine-utilizing species. We demonstrated that only one of two
Methanosarcina barkeri aRF1 homologs possesses activity and recognizes all three stop codons. The second aRF1 homolog may have another unknown function. The mechanism of pyrrolysine incorporation in the
Methanosarcinaceae is discussed.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2009.09.044</identifier><identifier>PMID: 19796638</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Archaea ; Archaeal Proteins - chemistry ; Archaeal Proteins - metabolism ; Archeon ; aRF1 ; Codon, Terminator - genetics ; Codon, Terminator - metabolism ; Genome, Archaeal ; Humans ; Lysine - analogs & derivatives ; Lysine - metabolism ; Methanosarcina barkeri ; Methanosarcinaceae ; Methanosarcinaceae - genetics ; Methanosarcinaceae - metabolism ; Molecular Sequence Data ; Peptide Termination Factors - chemistry ; Peptide Termination Factors - metabolism ; Phylogeny ; Polypeptide release factor ; Protein Biosynthesis ; Pyrrolysine-utilizing archea ; Translation termination</subject><ispartof>FEBS letters, 2009-11, Vol.583 (21), p.3455-3460</ispartof><rights>2009 Federation of European Biochemical Societies</rights><rights>FEBS Letters 583 (2009) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5623-b233a05b960914652baedf8e40455c5c804eedd5a8e16347becf8c818534a33e3</citedby><cites>FETCH-LOGICAL-c5623-b233a05b960914652baedf8e40455c5c804eedd5a8e16347becf8c818534a33e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2009.09.044$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579309007443$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,1411,1427,3537,27901,27902,45550,45551,46384,46808,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19796638$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Alkalaeva, Elena</creatorcontrib><creatorcontrib>Eliseev, Boris</creatorcontrib><creatorcontrib>Ambrogelly, Alexandre</creatorcontrib><creatorcontrib>Vlasov, Peter</creatorcontrib><creatorcontrib>Kondrashov, Fyodor A.</creatorcontrib><creatorcontrib>Gundllapalli, Sharath</creatorcontrib><creatorcontrib>Frolova, Lyudmila</creatorcontrib><creatorcontrib>Söll, Dieter</creatorcontrib><creatorcontrib>Kisselev, Lev</creatorcontrib><title>Translation termination in pyrrolysine-utilizing archaea</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Although some data link archaeal and eukaryotic translation, the overall mechanism of protein synthesis in archaea remains largely obscure. Both archaeal (aRF1) and eukaryotic (eRF1) single release factors recognize all three stop codons. The archaeal genus
Methanosarcinaceae contains two aRF1 homologs, and also uses the UAG stop to encode the 22nd amino acid, pyrrolysine. Here we provide an analysis of the last stage of archaeal translation in pyrrolysine-utilizing species. We demonstrated that only one of two
Methanosarcina barkeri aRF1 homologs possesses activity and recognizes all three stop codons. The second aRF1 homolog may have another unknown function. The mechanism of pyrrolysine incorporation in the
Methanosarcinaceae is discussed.</description><subject>Amino Acid Sequence</subject><subject>Archaea</subject><subject>Archaeal Proteins - chemistry</subject><subject>Archaeal Proteins - metabolism</subject><subject>Archeon</subject><subject>aRF1</subject><subject>Codon, Terminator - genetics</subject><subject>Codon, Terminator - metabolism</subject><subject>Genome, Archaeal</subject><subject>Humans</subject><subject>Lysine - analogs & derivatives</subject><subject>Lysine - metabolism</subject><subject>Methanosarcina barkeri</subject><subject>Methanosarcinaceae</subject><subject>Methanosarcinaceae - genetics</subject><subject>Methanosarcinaceae - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Peptide Termination Factors - chemistry</subject><subject>Peptide Termination Factors - metabolism</subject><subject>Phylogeny</subject><subject>Polypeptide release factor</subject><subject>Protein Biosynthesis</subject><subject>Pyrrolysine-utilizing archea</subject><subject>Translation termination</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1v1DAQhi0EosvCTwDtiZ6yjGM7ti8gWrUUqVIPlLPlOJPWK6-z2Nmi5dfjKCs-LlBpJNuad17PzEPIawprCrR5t1n32OaA47oG0OspOH9CFlRJVjHeqKdkAUB5JaRmJ-RFzhsob0X1c3JCtdRNw9SCqNtkYw529ENcjZi2Ps53H1e7Q0pDOGQfsdqPPvgfPt6tbHL3Fu1L8qy3IeOr47kkXy8vbs-vquubT5_PP15XTjQ1q9qaMQui1Q1oyhtRtxa7XiEHLoQTTgFH7DphFdKGcdmi65VTVAnGLWPIluT97Lvbt1vsHMYx2WB2yW9tOpjBevN3Jvp7czc8mFoJKagsBqdHgzR822MezdZnhyHYiMM-G8mYBlmXLS3J238qawpq2mwRilno0pBzwv5XOxTMRMdszJGOmeiYKTgvdW_-nOV31RFHEVzNgu8-4OFxruby4qz-MqGeSIMGkOWrYvVhtsIC58FjMtl5jA47n9CNphv8f7r9CZtHumk</recordid><startdate>20091103</startdate><enddate>20091103</enddate><creator>Alkalaeva, Elena</creator><creator>Eliseev, Boris</creator><creator>Ambrogelly, Alexandre</creator><creator>Vlasov, Peter</creator><creator>Kondrashov, Fyodor A.</creator><creator>Gundllapalli, Sharath</creator><creator>Frolova, Lyudmila</creator><creator>Söll, Dieter</creator><creator>Kisselev, Lev</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20091103</creationdate><title>Translation termination in pyrrolysine-utilizing archaea</title><author>Alkalaeva, Elena ; 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Both archaeal (aRF1) and eukaryotic (eRF1) single release factors recognize all three stop codons. The archaeal genus
Methanosarcinaceae contains two aRF1 homologs, and also uses the UAG stop to encode the 22nd amino acid, pyrrolysine. Here we provide an analysis of the last stage of archaeal translation in pyrrolysine-utilizing species. We demonstrated that only one of two
Methanosarcina barkeri aRF1 homologs possesses activity and recognizes all three stop codons. The second aRF1 homolog may have another unknown function. The mechanism of pyrrolysine incorporation in the
Methanosarcinaceae is discussed.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>19796638</pmid><doi>10.1016/j.febslet.2009.09.044</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Wiley Online Library Free Content; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Archaea Archaeal Proteins - chemistry Archaeal Proteins - metabolism Archeon aRF1 Codon, Terminator - genetics Codon, Terminator - metabolism Genome, Archaeal Humans Lysine - analogs & derivatives Lysine - metabolism Methanosarcina barkeri Methanosarcinaceae Methanosarcinaceae - genetics Methanosarcinaceae - metabolism Molecular Sequence Data Peptide Termination Factors - chemistry Peptide Termination Factors - metabolism Phylogeny Polypeptide release factor Protein Biosynthesis Pyrrolysine-utilizing archea Translation termination |
| title | Translation termination in pyrrolysine-utilizing archaea |
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