Codon Selection Affects Recruitment of Ribosome-Associating Factors during Translation
An intriguing aspect of protein synthesis is how cotranslational events are managed inside the cell. In this study, we developed an in vivo bimolecular fluorescence complementation assay coupled to SecM stalling (BiFC-SecM) to study how codon usage influences the interactions of ribosome-associating...
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Published in | ACS synthetic biology Vol. 9; no. 2; pp. 329 - 342 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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American Chemical Society
21.02.2020
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Abstract | An intriguing aspect of protein synthesis is how cotranslational events are managed inside the cell. In this study, we developed an in vivo bimolecular fluorescence complementation assay coupled to SecM stalling (BiFC-SecM) to study how codon usage influences the interactions of ribosome-associating factors that occur cotranslationally. We profiled ribosomal associations of a number of proteins, and observed differential association of chaperone proteins TF, DnaK, GroEL, and translocation factor Ffh as a result of introducing synonymous codon substitutions that change the affinity of the translating sequence to the ribosomal anti-Shine–Dalgarno (aSD) sequence. The use of pausing sequences within proteins regulates their transit within the translating ribosome. Our results indicate that the dynamics between cellular factors and the new polypeptide chain are affected by how codon composition is designed. Furthermore, associating factors may play a role in processes including protein quality control (folding and degradation) and cellular respiration. |
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AbstractList | An intriguing aspect of protein synthesis is how cotranslational events are managed inside the cell. In this study, we developed an
bimolecular fluorescence complementation assay coupled to SecM stalling (BiFC-SecM) to study how codon usage influences the interactions of ribosome-associating factors that occur cotranslationally. We profiled ribosomal associations of a number of proteins, and observed differential association of chaperone proteins TF, DnaK, GroEL, and translocation factor Ffh as a result of introducing synonymous codon substitutions that change the affinity of the translating sequence to the ribosomal anti-Shine-Dalgarno (aSD) sequence. The use of pausing sequences within proteins regulates their transit within the translating ribosome. Our results indicate that the dynamics between cellular factors and the new polypeptide chain are affected by how codon composition is designed. Furthermore, associating factors may play a role in processes including protein quality control (folding and degradation) and cellular respiration. An intriguing aspect of protein synthesis is how cotranslational events are managed inside the cell. In this study, we developed an in vivo bimolecular fluorescence complementation assay coupled to SecM stalling (BiFC-SecM) to study how codon usage influences the interactions of ribosome-associating factors that occur cotranslationally. We profiled ribosomal associations of a number of proteins, and observed differential association of chaperone proteins TF, DnaK, GroEL, and translocation factor Ffh as a result of introducing synonymous codon substitutions that change the affinity of the translating sequence to the ribosomal anti-Shine–Dalgarno (aSD) sequence. The use of pausing sequences within proteins regulates their transit within the translating ribosome. Our results indicate that the dynamics between cellular factors and the new polypeptide chain are affected by how codon composition is designed. Furthermore, associating factors may play a role in processes including protein quality control (folding and degradation) and cellular respiration. |
Author | Rojano-Nisimura, Alejandra M Haning, Katie Janovsky, Justin Thompson, Jeffrey P Contreras, Lydia M Vasquez, Kevin A |
AuthorAffiliation | Institute for Cellular and Molecular Biology McKetta Department of Chemical Engineering |
AuthorAffiliation_xml | – name: Institute for Cellular and Molecular Biology – name: McKetta Department of Chemical Engineering |
Author_xml | – sequence: 1 givenname: Alejandra M surname: Rojano-Nisimura fullname: Rojano-Nisimura, Alejandra M organization: Institute for Cellular and Molecular Biology – sequence: 2 givenname: Katie surname: Haning fullname: Haning, Katie organization: McKetta Department of Chemical Engineering – sequence: 3 givenname: Justin surname: Janovsky fullname: Janovsky, Justin organization: Institute for Cellular and Molecular Biology – sequence: 4 givenname: Kevin A surname: Vasquez fullname: Vasquez, Kevin A organization: McKetta Department of Chemical Engineering – sequence: 5 givenname: Jeffrey P surname: Thompson fullname: Thompson, Jeffrey P organization: McKetta Department of Chemical Engineering – sequence: 6 givenname: Lydia M orcidid: 0000-0001-5010-5511 surname: Contreras fullname: Contreras, Lydia M email: lcontrer@che.utexas.edu organization: McKetta Department of Chemical Engineering |
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Snippet | An intriguing aspect of protein synthesis is how cotranslational events are managed inside the cell. In this study, we developed an in vivo bimolecular... An intriguing aspect of protein synthesis is how cotranslational events are managed inside the cell. In this study, we developed an bimolecular fluorescence... |
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SubjectTerms | Bacterial Proteins - biosynthesis Bacterial Proteins - genetics Codon - metabolism Escherichia coli - metabolism Luminescent Proteins - biosynthesis Luminescent Proteins - genetics Molecular Chaperones - metabolism Protein Biosynthesis Ribosomal Proteins - metabolism Ribosomes - metabolism RNA, Messenger - metabolism Signal Recognition Particle - metabolism |
Title | Codon Selection Affects Recruitment of Ribosome-Associating Factors during Translation |
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