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

Gespeichert in:

Autor*in:	Milin, Anthony [verfasserIn] Goldman, Daniel H Righini, Maurizio Kaiser, Christian M Bustamante, Carlos Tinoco, Jr, Ignacio

Format:	Artikel
Sprache:	Englisch

Erschienen:	2015

Rechteinformationen:	Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science.

Schlagwörter:	Transcription Factors - biosynthesis Escherichia coli Proteins - biosynthesis Escherichia coli - metabolism Escherichia coli Proteins - chemistry Transcription Factors - chemistry Ribosomes - chemistry Ribosomes - metabolism

Übergeordnetes Werk:	Enthalten in: Science - Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883, 348(2015), 6233, Seite 457
Übergeordnetes Werk:	volume:348 ; year:2015 ; number:6233 ; pages:457

Links:	Link aufrufen

Katalog-ID:	OLC1969520833

Internformat


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245	1	0	\|a Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo
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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
773	0	8	\|i Enthalten in \|t Science \|d Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 \|g 348(2015), 6233, Seite 457 \|w (DE-627)12931482X \|w (DE-600)128410-1 \|w (DE-576)014533189 \|x 0036-8075 \|7 nnns
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912			\|a GBV_ILN_20
912			\|a GBV_ILN_21
912			\|a GBV_ILN_22
912			\|a GBV_ILN_23
912			\|a GBV_ILN_24
912			\|a GBV_ILN_30
912			\|a GBV_ILN_31
912			\|a GBV_ILN_39
912			\|a GBV_ILN_40
912			\|a GBV_ILN_47
912			\|a GBV_ILN_55
912			\|a GBV_ILN_59
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_92
912			\|a GBV_ILN_101
912			\|a GBV_ILN_110
912			\|a GBV_ILN_120
912			\|a GBV_ILN_131
912			\|a GBV_ILN_170
912			\|a GBV_ILN_171
912			\|a GBV_ILN_179
912			\|a GBV_ILN_181
912			\|a GBV_ILN_211
912			\|a GBV_ILN_252
912			\|a GBV_ILN_259
912			\|a GBV_ILN_290
912			\|a GBV_ILN_600
912			\|a GBV_ILN_601
912			\|a GBV_ILN_647
912			\|a GBV_ILN_754
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2008
912			\|a GBV_ILN_2012
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2018
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2116
912			\|a GBV_ILN_2120
912			\|a GBV_ILN_2121
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912			\|a GBV_ILN_2219
912			\|a GBV_ILN_2221
912			\|a GBV_ILN_2279
912			\|a GBV_ILN_2286
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4036
912			\|a GBV_ILN_4046
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4219
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4277
912			\|a GBV_ILN_4302
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4310
912			\|a GBV_ILN_4314
912			\|a GBV_ILN_4317
912			\|a GBV_ILN_4318
912			\|a GBV_ILN_4320
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4328
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4700
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952			\|d 348 \|j 2015 \|e 6233 \|h 457

Indexfelder

author_variant	a m am
matchkey_str	article:00368075:2015----::iooeehnclocrlaensethimdaerbsma
hierarchy_sort_str	2015
publishDate	2015
allfields	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
allfieldsSound	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
language	English
source	Enthalten in Science 348(2015), 6233, Seite 457 volume:348 year:2015 number:6233 pages:457
sourceStr	Enthalten in Science 348(2015), 6233, Seite 457 volume:348 year:2015 number:6233 pages:457
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Transcription Factors - biosynthesis Escherichia coli Proteins - biosynthesis Escherichia coli - metabolism Escherichia coli Proteins - chemistry Transcription Factors - chemistry Ribosomes - chemistry Ribosomes - metabolism
dewey-raw	500
isfreeaccess_bool	false
container_title	Science
authorswithroles_txt_mv	Milin, Anthony @@aut@@ Goldman, Daniel H @@oth@@ Righini, Maurizio @@oth@@ Kaiser, Christian M @@oth@@ Bustamante, Carlos @@oth@@ Tinoco, Jr, Ignacio @@oth@@
publishDateDaySort_date	2015-01-01T00:00:00Z
hierarchy_top_id	12931482X
dewey-sort	3500
id	OLC1969520833
language_de	englisch
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author	Milin, Anthony
spellingShingle	Milin, Anthony 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 Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo
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topic_title	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
topic	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
topic_unstemmed	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
ctrlnum	(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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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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container_issue	6233
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	false
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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Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo

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