Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo
Protein synthesis rates can affect gene expression and the folding and activity of the translation product. Interactions between the nascent polypeptide and the ribosome exit tunnel represent one mode of regulating synthesis rates. The SecM protein arrests its own translation, and release of arrest...
Ausführliche Beschreibung
Autor*in: |
Milin, Anthony [verfasserIn] |
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Format: |
Artikel |
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Sprache: |
Englisch |
Erschienen: |
2015 |
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Rechteinformationen: |
Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. |
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Schlagwörter: |
Transcription Factors - biosynthesis Escherichia coli Proteins - biosynthesis Escherichia coli Proteins - chemistry |
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Übergeordnetes Werk: |
Enthalten in: Science - Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883, 348(2015), 6233, Seite 457 |
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Übergeordnetes Werk: |
volume:348 ; year:2015 ; number:6233 ; pages:457 |
Links: |
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Katalog-ID: |
OLC1969520833 |
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520 | |a Protein synthesis rates can affect gene expression and the folding and activity of the translation product. Interactions between the nascent polypeptide and the ribosome exit tunnel represent one mode of regulating synthesis rates. The SecM protein arrests its own translation, and release of arrest at the translocon has been proposed to occur by mechanical force. Using optical tweezers, we demonstrate that arrest of SecM-stalled ribosomes can indeed be rescued by force alone and that the force needed to release stalling can be generated in vivo by a nascent chain folding near the ribosome tunnel exit. We formulate a kinetic model describing how a protein can regulate its own synthesis by the force generated during folding, tuning ribosome activity to structure acquisition by a nascent polypeptide. | ||
540 | |a Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. | ||
650 | 4 | |a Transcription Factors - biosynthesis | |
650 | 4 | |a Escherichia coli Proteins - biosynthesis | |
650 | 4 | |a Escherichia coli - metabolism | |
650 | 4 | |a Escherichia coli Proteins - chemistry | |
650 | 4 | |a Transcription Factors - chemistry | |
650 | 4 | |a Ribosomes - chemistry | |
650 | 4 | |a Ribosomes - metabolism | |
700 | 1 | |a Goldman, Daniel H |4 oth | |
700 | 1 | |a Righini, Maurizio |4 oth | |
700 | 1 | |a Kaiser, Christian M |4 oth | |
700 | 1 | |a Bustamante, Carlos |4 oth | |
700 | 1 | |a Tinoco, Jr, Ignacio |4 oth | |
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PQ20160211 (DE-627)OLC1969520833 (DE-599)GBVOLC1969520833 (PRQ)pubmed_primary_259088240 (KEY)0063888920150000348623300457ribosomemechanicalforcereleasesnascentchainmediate DE-627 ger DE-627 rakwb eng 500 DNB LING fid Milin, Anthony verfasserin aut Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Protein synthesis rates can affect gene expression and the folding and activity of the translation product. Interactions between the nascent polypeptide and the ribosome exit tunnel represent one mode of regulating synthesis rates. The SecM protein arrests its own translation, and release of arrest at the translocon has been proposed to occur by mechanical force. Using optical tweezers, we demonstrate that arrest of SecM-stalled ribosomes can indeed be rescued by force alone and that the force needed to release stalling can be generated in vivo by a nascent chain folding near the ribosome tunnel exit. We formulate a kinetic model describing how a protein can regulate its own synthesis by the force generated during folding, tuning ribosome activity to structure acquisition by a nascent polypeptide. Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. Transcription Factors - biosynthesis Escherichia coli Proteins - biosynthesis Escherichia coli - metabolism Escherichia coli Proteins - chemistry Transcription Factors - chemistry Ribosomes - chemistry Ribosomes - metabolism Goldman, Daniel H oth Righini, Maurizio oth Kaiser, Christian M oth Bustamante, Carlos oth Tinoco, Jr, Ignacio oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 348(2015), 6233, Seite 457 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:348 year:2015 number:6233 pages:457 http://www.ncbi.nlm.nih.gov/pubmed/25908824 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2185 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 348 2015 6233 457 |
spelling |
PQ20160211 (DE-627)OLC1969520833 (DE-599)GBVOLC1969520833 (PRQ)pubmed_primary_259088240 (KEY)0063888920150000348623300457ribosomemechanicalforcereleasesnascentchainmediate DE-627 ger DE-627 rakwb eng 500 DNB LING fid Milin, Anthony verfasserin aut Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Protein synthesis rates can affect gene expression and the folding and activity of the translation product. Interactions between the nascent polypeptide and the ribosome exit tunnel represent one mode of regulating synthesis rates. The SecM protein arrests its own translation, and release of arrest at the translocon has been proposed to occur by mechanical force. Using optical tweezers, we demonstrate that arrest of SecM-stalled ribosomes can indeed be rescued by force alone and that the force needed to release stalling can be generated in vivo by a nascent chain folding near the ribosome tunnel exit. We formulate a kinetic model describing how a protein can regulate its own synthesis by the force generated during folding, tuning ribosome activity to structure acquisition by a nascent polypeptide. Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. Transcription Factors - biosynthesis Escherichia coli Proteins - biosynthesis Escherichia coli - metabolism Escherichia coli Proteins - chemistry Transcription Factors - chemistry Ribosomes - chemistry Ribosomes - metabolism Goldman, Daniel H oth Righini, Maurizio oth Kaiser, Christian M oth Bustamante, Carlos oth Tinoco, Jr, Ignacio oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 348(2015), 6233, Seite 457 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:348 year:2015 number:6233 pages:457 http://www.ncbi.nlm.nih.gov/pubmed/25908824 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2185 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 348 2015 6233 457 |
allfields_unstemmed |
PQ20160211 (DE-627)OLC1969520833 (DE-599)GBVOLC1969520833 (PRQ)pubmed_primary_259088240 (KEY)0063888920150000348623300457ribosomemechanicalforcereleasesnascentchainmediate DE-627 ger DE-627 rakwb eng 500 DNB LING fid Milin, Anthony verfasserin aut Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Protein synthesis rates can affect gene expression and the folding and activity of the translation product. Interactions between the nascent polypeptide and the ribosome exit tunnel represent one mode of regulating synthesis rates. The SecM protein arrests its own translation, and release of arrest at the translocon has been proposed to occur by mechanical force. Using optical tweezers, we demonstrate that arrest of SecM-stalled ribosomes can indeed be rescued by force alone and that the force needed to release stalling can be generated in vivo by a nascent chain folding near the ribosome tunnel exit. We formulate a kinetic model describing how a protein can regulate its own synthesis by the force generated during folding, tuning ribosome activity to structure acquisition by a nascent polypeptide. Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. Transcription Factors - biosynthesis Escherichia coli Proteins - biosynthesis Escherichia coli - metabolism Escherichia coli Proteins - chemistry Transcription Factors - chemistry Ribosomes - chemistry Ribosomes - metabolism Goldman, Daniel H oth Righini, Maurizio oth Kaiser, Christian M oth Bustamante, Carlos oth Tinoco, Jr, Ignacio oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 348(2015), 6233, Seite 457 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:348 year:2015 number:6233 pages:457 http://www.ncbi.nlm.nih.gov/pubmed/25908824 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2185 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 348 2015 6233 457 |
allfieldsGer |
PQ20160211 (DE-627)OLC1969520833 (DE-599)GBVOLC1969520833 (PRQ)pubmed_primary_259088240 (KEY)0063888920150000348623300457ribosomemechanicalforcereleasesnascentchainmediate DE-627 ger DE-627 rakwb eng 500 DNB LING fid Milin, Anthony verfasserin aut Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Protein synthesis rates can affect gene expression and the folding and activity of the translation product. Interactions between the nascent polypeptide and the ribosome exit tunnel represent one mode of regulating synthesis rates. The SecM protein arrests its own translation, and release of arrest at the translocon has been proposed to occur by mechanical force. Using optical tweezers, we demonstrate that arrest of SecM-stalled ribosomes can indeed be rescued by force alone and that the force needed to release stalling can be generated in vivo by a nascent chain folding near the ribosome tunnel exit. We formulate a kinetic model describing how a protein can regulate its own synthesis by the force generated during folding, tuning ribosome activity to structure acquisition by a nascent polypeptide. Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. Transcription Factors - biosynthesis Escherichia coli Proteins - biosynthesis Escherichia coli - metabolism Escherichia coli Proteins - chemistry Transcription Factors - chemistry Ribosomes - chemistry Ribosomes - metabolism Goldman, Daniel H oth Righini, Maurizio oth Kaiser, Christian M oth Bustamante, Carlos oth Tinoco, Jr, Ignacio oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 348(2015), 6233, Seite 457 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:348 year:2015 number:6233 pages:457 http://www.ncbi.nlm.nih.gov/pubmed/25908824 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2185 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 348 2015 6233 457 |
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PQ20160211 (DE-627)OLC1969520833 (DE-599)GBVOLC1969520833 (PRQ)pubmed_primary_259088240 (KEY)0063888920150000348623300457ribosomemechanicalforcereleasesnascentchainmediate DE-627 ger DE-627 rakwb eng 500 DNB LING fid Milin, Anthony verfasserin aut Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Protein synthesis rates can affect gene expression and the folding and activity of the translation product. Interactions between the nascent polypeptide and the ribosome exit tunnel represent one mode of regulating synthesis rates. The SecM protein arrests its own translation, and release of arrest at the translocon has been proposed to occur by mechanical force. Using optical tweezers, we demonstrate that arrest of SecM-stalled ribosomes can indeed be rescued by force alone and that the force needed to release stalling can be generated in vivo by a nascent chain folding near the ribosome tunnel exit. We formulate a kinetic model describing how a protein can regulate its own synthesis by the force generated during folding, tuning ribosome activity to structure acquisition by a nascent polypeptide. Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. Transcription Factors - biosynthesis Escherichia coli Proteins - biosynthesis Escherichia coli - metabolism Escherichia coli Proteins - chemistry Transcription Factors - chemistry Ribosomes - chemistry Ribosomes - metabolism Goldman, Daniel H oth Righini, Maurizio oth Kaiser, Christian M oth Bustamante, Carlos oth Tinoco, Jr, Ignacio oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 348(2015), 6233, Seite 457 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:348 year:2015 number:6233 pages:457 http://www.ncbi.nlm.nih.gov/pubmed/25908824 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2185 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 348 2015 6233 457 |
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Enthalten in Science 348(2015), 6233, Seite 457 volume:348 year:2015 number:6233 pages:457 |
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Milin, Anthony @@aut@@ Goldman, Daniel H @@oth@@ Righini, Maurizio @@oth@@ Kaiser, Christian M @@oth@@ Bustamante, Carlos @@oth@@ Tinoco, Jr, Ignacio @@oth@@ |
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500 DNB LING fid Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo Transcription Factors - biosynthesis Escherichia coli Proteins - biosynthesis Escherichia coli - metabolism Escherichia coli Proteins - chemistry Transcription Factors - chemistry Ribosomes - chemistry Ribosomes - metabolism |
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ddc 500 fid LING misc Transcription Factors - biosynthesis misc Escherichia coli Proteins - biosynthesis misc Escherichia coli - metabolism misc Escherichia coli Proteins - chemistry misc Transcription Factors - chemistry misc Ribosomes - chemistry misc Ribosomes - metabolism |
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ddc 500 fid LING misc Transcription Factors - biosynthesis misc Escherichia coli Proteins - biosynthesis misc Escherichia coli - metabolism misc Escherichia coli Proteins - chemistry misc Transcription Factors - chemistry misc Ribosomes - chemistry misc Ribosomes - metabolism |
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ddc 500 fid LING misc Transcription Factors - biosynthesis misc Escherichia coli Proteins - biosynthesis misc Escherichia coli - metabolism misc Escherichia coli Proteins - chemistry misc Transcription Factors - chemistry misc Ribosomes - chemistry misc Ribosomes - metabolism |
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title |
Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo |
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(DE-627)OLC1969520833 (DE-599)GBVOLC1969520833 (PRQ)pubmed_primary_259088240 (KEY)0063888920150000348623300457ribosomemechanicalforcereleasesnascentchainmediate |
title_full |
Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo |
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Milin, Anthony |
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title_sort |
ribosome. mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo |
title_auth |
Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo |
abstract |
Protein synthesis rates can affect gene expression and the folding and activity of the translation product. Interactions between the nascent polypeptide and the ribosome exit tunnel represent one mode of regulating synthesis rates. The SecM protein arrests its own translation, and release of arrest at the translocon has been proposed to occur by mechanical force. Using optical tweezers, we demonstrate that arrest of SecM-stalled ribosomes can indeed be rescued by force alone and that the force needed to release stalling can be generated in vivo by a nascent chain folding near the ribosome tunnel exit. We formulate a kinetic model describing how a protein can regulate its own synthesis by the force generated during folding, tuning ribosome activity to structure acquisition by a nascent polypeptide. |
abstractGer |
Protein synthesis rates can affect gene expression and the folding and activity of the translation product. Interactions between the nascent polypeptide and the ribosome exit tunnel represent one mode of regulating synthesis rates. The SecM protein arrests its own translation, and release of arrest at the translocon has been proposed to occur by mechanical force. Using optical tweezers, we demonstrate that arrest of SecM-stalled ribosomes can indeed be rescued by force alone and that the force needed to release stalling can be generated in vivo by a nascent chain folding near the ribosome tunnel exit. We formulate a kinetic model describing how a protein can regulate its own synthesis by the force generated during folding, tuning ribosome activity to structure acquisition by a nascent polypeptide. |
abstract_unstemmed |
Protein synthesis rates can affect gene expression and the folding and activity of the translation product. Interactions between the nascent polypeptide and the ribosome exit tunnel represent one mode of regulating synthesis rates. The SecM protein arrests its own translation, and release of arrest at the translocon has been proposed to occur by mechanical force. Using optical tweezers, we demonstrate that arrest of SecM-stalled ribosomes can indeed be rescued by force alone and that the force needed to release stalling can be generated in vivo by a nascent chain folding near the ribosome tunnel exit. We formulate a kinetic model describing how a protein can regulate its own synthesis by the force generated during folding, tuning ribosome activity to structure acquisition by a nascent polypeptide. |
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title_short |
Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo |
url |
http://www.ncbi.nlm.nih.gov/pubmed/25908824 |
remote_bool |
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author2 |
Goldman, Daniel H Righini, Maurizio Kaiser, Christian M Bustamante, Carlos Tinoco, Jr, Ignacio |
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up_date |
2024-07-04T05:42:16.802Z |
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