Publication Date:
2015-04-25
Description:
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.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4618485/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4618485/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldman, Daniel H -- Kaiser, Christian M -- Milin, Anthony -- Righini, Maurizio -- Tinoco, Ignacio Jr -- Bustamante, Carlos -- 5K99GM086516/GM/NIGMS NIH HHS/ -- 5R01GM32543/GM/NIGMS NIH HHS/ -- GM10840/GM/NIGMS NIH HHS/ -- K99 GM086516/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2015 Apr 24;348(6233):457-60. doi: 10.1126/science.1261909. Epub 2015 Apr 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley, CA 94720, USA. ; Institute for Quantitative Biosciences (QB3), University of California, Berkeley, CA 94720, USA. Department of Biology, Johns Hopkins University, Baltimore, MD 21218, USA. carlos@alice.berkeley.edu kaiser@jhu.edu. ; Department of Chemistry, University of California, Berkeley, CA 94720, USA. Department of Biology, Johns Hopkins University, Baltimore, MD 21218, USA. ; Institute for Quantitative Biosciences (QB3), University of California, Berkeley, CA 94720, USA. ; Department of Chemistry, University of California, Berkeley, CA 94720, USA. Institute for Quantitative Biosciences (QB3), University of California, Berkeley, CA 94720, USA. Department of Physics, University of California, Berkeley, CA 94720, USA. Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA. Kavli Energy Nanosciences Institute at Berkeley, Berkeley, CA 94720, USA. Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA. carlos@alice.berkeley.edu kaiser@jhu.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25908824" target="_blank"〉PubMed〈/a〉
Keywords:
Escherichia coli/*metabolism
;
Escherichia coli Proteins/*biosynthesis/*chemistry
;
In Vitro Techniques
;
Kinetics
;
Mechanical Processes
;
Optical Tweezers
;
*Peptide Chain Elongation, Translational
;
*Protein Folding
;
Ribosomes/chemistry/*metabolism
;
Transcription Factors/*biosynthesis/*chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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