The phenotype of many independently isolated +1 frameshift suppressor mutants supports a pivotal role of the P-site in reading frame maintenance
The main features of translation are similar in all organisms on this planet and one important feature of it is the way the ribosome maintain the reading frame. We have earlier characterized several bacterial mutants defective in tRNA maturation and found that some of them correct a +1 frameshift mu...
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| description | The main features of translation are similar in all organisms on this planet and one important feature of it is the way the ribosome maintain the reading frame. We have earlier characterized several bacterial mutants defective in tRNA maturation and found that some of them correct a +1 frameshift mutation; i.e. such mutants possess an error in reading frame maintenance. Based on the analysis of the frameshifting phenotype of such mutants we proposed a pivotal role of the ribosomal grip of the peptidyl-tRNA to maintain the correct reading frame. To test the model in an unbiased way we first isolated many (467) independent mutants able to correct a +1 frameshift mutation and thereafter tested whether or not their frameshifting phenotypes were consistent with the model. These 467+1 frameshift suppressor mutants had alterations in 16 different loci of which 15 induced a defective tRNA by hypo- or hypermodifications or altering its primary sequence. All these alterations of tRNAs induce a frameshift error in the P-site to correct a +1 frameshift mutation consistent with the proposed model. Modifications next to and 3' of the anticodon (position 37), like 1-methylguanosine, are important for proper reading frame maintenance due to their interactions with components of the ribosomal P-site. Interestingly, two mutants had a defect in a locus (rpsI), which encodes ribosomal protein S9. The C-terminal of this protein contacts position 32-34 of the peptidyl-tRNA and is thus part of the P-site environment. The two rpsI mutants had a C-terminal truncated ribosomal protein S9 that destroys its interaction with the peptidyl-tRNA resulting in +1 shift in the reading frame. The isolation and characterization of the S9 mutants gave strong support of our model that the ribosomal grip of the peptidyl-tRNA is pivotal for the reading frame maintenance. |
| doi_str_mv | 10.1371/journal.pone.0060246 |
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We have earlier characterized several bacterial mutants defective in tRNA maturation and found that some of them correct a +1 frameshift mutation; i.e. such mutants possess an error in reading frame maintenance. Based on the analysis of the frameshifting phenotype of such mutants we proposed a pivotal role of the ribosomal grip of the peptidyl-tRNA to maintain the correct reading frame. To test the model in an unbiased way we first isolated many (467) independent mutants able to correct a +1 frameshift mutation and thereafter tested whether or not their frameshifting phenotypes were consistent with the model. These 467+1 frameshift suppressor mutants had alterations in 16 different loci of which 15 induced a defective tRNA by hypo- or hypermodifications or altering its primary sequence. All these alterations of tRNAs induce a frameshift error in the P-site to correct a +1 frameshift mutation consistent with the proposed model. Modifications next to and 3' of the anticodon (position 37), like 1-methylguanosine, are important for proper reading frame maintenance due to their interactions with components of the ribosomal P-site. Interestingly, two mutants had a defect in a locus (rpsI), which encodes ribosomal protein S9. The C-terminal of this protein contacts position 32-34 of the peptidyl-tRNA and is thus part of the P-site environment. The two rpsI mutants had a C-terminal truncated ribosomal protein S9 that destroys its interaction with the peptidyl-tRNA resulting in +1 shift in the reading frame. The isolation and characterization of the S9 mutants gave strong support of our model that the ribosomal grip of the peptidyl-tRNA is pivotal for the reading frame maintenance.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0060246</identifier><identifier>PMID: 23593181</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Alterations ; Amino Acid Sequence ; Anticodon ; Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Base Sequence ; Biology ; Codon ; Defects ; E coli ; Error correction ; Escherichia coli ; Frameshift Mutation ; Gene mutations ; Loci ; Maintenance ; Molecular biology ; Molecular Sequence Data ; Mutants ; Mutation ; Nucleic Acid Conformation ; Operon - physiology ; Phenotype ; Physiological aspects ; Protein Biosynthesis - physiology ; Proteins ; Reading ; Reading Frames ; Ribosomal protein S9 ; Ribosomal Proteins - chemistry ; Ribosomes - physiology ; RNA, Transfer, Amino Acyl - chemistry ; RNA, Transfer, Amino Acyl - physiology ; Salmonella ; Salmonella Typhimurium ; Transfer RNA ; tRNA</subject><ispartof>PloS one, 2013-04, Vol.8 (4), p.e60246-e60246</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Björk et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 Björk et al 2013 Björk et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c795t-6e582f92e43cb62853c6fcf55d76e133ebbf1da60caf8dcca3977f02ffbd10963</citedby><cites>FETCH-LOGICAL-c795t-6e582f92e43cb62853c6fcf55d76e133ebbf1da60caf8dcca3977f02ffbd10963</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3617221/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3617221/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,550,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79343,79344</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23593181$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-76815$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Jäger, Gunilla</creatorcontrib><creatorcontrib>Nilsson, Kristina</creatorcontrib><creatorcontrib>Björk, Glenn R</creatorcontrib><title>The phenotype of many independently isolated +1 frameshift suppressor mutants supports a pivotal role of the P-site in reading frame maintenance</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The main features of translation are similar in all organisms on this planet and one important feature of it is the way the ribosome maintain the reading frame. We have earlier characterized several bacterial mutants defective in tRNA maturation and found that some of them correct a +1 frameshift mutation; i.e. such mutants possess an error in reading frame maintenance. Based on the analysis of the frameshifting phenotype of such mutants we proposed a pivotal role of the ribosomal grip of the peptidyl-tRNA to maintain the correct reading frame. To test the model in an unbiased way we first isolated many (467) independent mutants able to correct a +1 frameshift mutation and thereafter tested whether or not their frameshifting phenotypes were consistent with the model. These 467+1 frameshift suppressor mutants had alterations in 16 different loci of which 15 induced a defective tRNA by hypo- or hypermodifications or altering its primary sequence. All these alterations of tRNAs induce a frameshift error in the P-site to correct a +1 frameshift mutation consistent with the proposed model. Modifications next to and 3' of the anticodon (position 37), like 1-methylguanosine, are important for proper reading frame maintenance due to their interactions with components of the ribosomal P-site. Interestingly, two mutants had a defect in a locus (rpsI), which encodes ribosomal protein S9. The C-terminal of this protein contacts position 32-34 of the peptidyl-tRNA and is thus part of the P-site environment. The two rpsI mutants had a C-terminal truncated ribosomal protein S9 that destroys its interaction with the peptidyl-tRNA resulting in +1 shift in the reading frame. The isolation and characterization of the S9 mutants gave strong support of our model that the ribosomal grip of the peptidyl-tRNA is pivotal for the reading frame maintenance.</description><subject>Alterations</subject><subject>Amino Acid Sequence</subject><subject>Anticodon</subject><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Base Sequence</subject><subject>Biology</subject><subject>Codon</subject><subject>Defects</subject><subject>E coli</subject><subject>Error correction</subject><subject>Escherichia coli</subject><subject>Frameshift Mutation</subject><subject>Gene mutations</subject><subject>Loci</subject><subject>Maintenance</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Nucleic Acid Conformation</subject><subject>Operon - physiology</subject><subject>Phenotype</subject><subject>Physiological aspects</subject><subject>Protein Biosynthesis - physiology</subject><subject>Proteins</subject><subject>Reading</subject><subject>Reading Frames</subject><subject>Ribosomal protein S9</subject><subject>Ribosomal Proteins - chemistry</subject><subject>Ribosomes - physiology</subject><subject>RNA, Transfer, Amino Acyl - chemistry</subject><subject>RNA, Transfer, Amino Acyl - physiology</subject><subject>Salmonella</subject><subject>Salmonella Typhimurium</subject><subject>Transfer RNA</subject><subject>tRNA</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>D8T</sourceid><sourceid>DOA</sourceid><recordid>eNqNk29r1TAUxosobk6_gWhBEEXvNWnatH0jXOa_wWCic2_DaXpyb0ab1CSd7lv4kc39s3EreyGFNk1_z3OaJzlJ8pSSOWUlfXdpR2egmw_W4JwQTrKc30sOac2yGc8Iu783PkgeeX9JSMEqzh8mBxkrakYrepj8OV9hOqzQ2HA9YGpV2oO5TrVpccB4M6GLb952ELBN39BUOejRr7QKqR-HwaH31qX9GMAEv5myLg4gHfSVDdClznYb3xALfZ15HTC6pw6h1Wa5tYs1tQlowEh8nDxQ0Hl8snseJT8-fTw__jI7Pft8crw4ncmyLsKMY1Flqs4wZ7LhWVUwyZVURdGWHClj2DSKtsCJBFW1UgKry1KRTKmmpaTm7Ch5vvUdOuvFLkwvopTUNKckj8TJlmgtXIrB6R7ctbCgxWbCuqUAF7TsUEgAzFXGm6Iuc9ZyAIKEN6hyXmQ0q6PX262X_4XD2EzcPuiLxcZt7EdR8ooWEX-_-7mx6bGVcRscdBPV9IvRK7G0V4JxWmYZjQavdgbO_hzRB9FrL7HrwKAd18uMkeWsIOsgXvyD3h3GjlpCXK82ysa6cm0qFnlZ5SznnERqfgcVrxZ7LeNBVTrOTwSvJ4LIBPwdljB6L06-f_t_9uxiyr7cY1cIXVjFQzwGbY2fgvkWlM5671DdhkyJWPfZTRpi3Wdi12dR9mx_g25FN43F_gJ-BCYh</recordid><startdate>20130404</startdate><enddate>20130404</enddate><creator>Jäger, Gunilla</creator><creator>Nilsson, Kristina</creator><creator>Björk, Glenn R</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>ADHXS</scope><scope>ADTPV</scope><scope>AOWAS</scope><scope>D8T</scope><scope>D93</scope><scope>ZZAVC</scope><scope>DOA</scope></search><sort><creationdate>20130404</creationdate><title>The phenotype of many independently isolated +1 frameshift suppressor mutants supports a pivotal role of the P-site in reading frame maintenance</title><author>Jäger, Gunilla ; Nilsson, Kristina ; Björk, Glenn R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c795t-6e582f92e43cb62853c6fcf55d76e133ebbf1da60caf8dcca3977f02ffbd10963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Alterations</topic><topic>Amino Acid Sequence</topic><topic>Anticodon</topic><topic>Bacteria</topic><topic>Bacterial Proteins - 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We have earlier characterized several bacterial mutants defective in tRNA maturation and found that some of them correct a +1 frameshift mutation; i.e. such mutants possess an error in reading frame maintenance. Based on the analysis of the frameshifting phenotype of such mutants we proposed a pivotal role of the ribosomal grip of the peptidyl-tRNA to maintain the correct reading frame. To test the model in an unbiased way we first isolated many (467) independent mutants able to correct a +1 frameshift mutation and thereafter tested whether or not their frameshifting phenotypes were consistent with the model. These 467+1 frameshift suppressor mutants had alterations in 16 different loci of which 15 induced a defective tRNA by hypo- or hypermodifications or altering its primary sequence. All these alterations of tRNAs induce a frameshift error in the P-site to correct a +1 frameshift mutation consistent with the proposed model. Modifications next to and 3' of the anticodon (position 37), like 1-methylguanosine, are important for proper reading frame maintenance due to their interactions with components of the ribosomal P-site. Interestingly, two mutants had a defect in a locus (rpsI), which encodes ribosomal protein S9. The C-terminal of this protein contacts position 32-34 of the peptidyl-tRNA and is thus part of the P-site environment. The two rpsI mutants had a C-terminal truncated ribosomal protein S9 that destroys its interaction with the peptidyl-tRNA resulting in +1 shift in the reading frame. The isolation and characterization of the S9 mutants gave strong support of our model that the ribosomal grip of the peptidyl-tRNA is pivotal for the reading frame maintenance.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23593181</pmid><doi>10.1371/journal.pone.0060246</doi><tpages>e60246</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Alterations Amino Acid Sequence Anticodon Bacteria Bacterial Proteins - chemistry Bacterial Proteins - genetics Base Sequence Biology Codon Defects E coli Error correction Escherichia coli Frameshift Mutation Gene mutations Loci Maintenance Molecular biology Molecular Sequence Data Mutants Mutation Nucleic Acid Conformation Operon - physiology Phenotype Physiological aspects Protein Biosynthesis - physiology Proteins Reading Reading Frames Ribosomal protein S9 Ribosomal Proteins - chemistry Ribosomes - physiology RNA, Transfer, Amino Acyl - chemistry RNA, Transfer, Amino Acyl - physiology Salmonella Salmonella Typhimurium Transfer RNA tRNA |
| title | The phenotype of many independently isolated +1 frameshift suppressor mutants supports a pivotal role of the P-site in reading frame maintenance |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-02T11%3A03%3A45IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20phenotype%20of%20many%20independently%20isolated%20+1%20frameshift%20suppressor%20mutants%20supports%20a%20pivotal%20role%20of%20the%20P-site%20in%20reading%20frame%20maintenance&rft.jtitle=PloS%20one&rft.au=J%C3%A4ger,%20Gunilla&rft.date=2013-04-04&rft.volume=8&rft.issue=4&rft.spage=e60246&rft.epage=e60246&rft.pages=e60246-e60246&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0060246&rft_dat=%3Cgale_plos_%3EA478434660%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1330914104&rft_id=info:pmid/23593181&rft_galeid=A478434660&rft_doaj_id=oai_doaj_org_article_caae4f26b59743d6aa0e06bef4652129&rfr_iscdi=true |