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 inACS synthetic biology Vol. 9; no. 2; pp. 329 - 342
Main Authors Rojano-Nisimura, Alejandra M, Haning, Katie, Janovsky, Justin, Vasquez, Kevin A, Thompson, Jeffrey P, Contreras, Lydia M
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 21.02.2020
Subjects
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
translation pausing
translation regulation
protein chaperones
ribosome-associated factors
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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.
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
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CitedBy_id crossref_primary_10_1016_j_tibtech_2021_10_010
crossref_primary_10_1128_spectrum_02140_22
crossref_primary_10_1016_j_synbio_2020_05_002
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translation regulation
protein chaperones
ribosome-associated factors
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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
URI http://dx.doi.org/10.1021/acssynbio.9b00344
https://www.ncbi.nlm.nih.gov/pubmed/31769967
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