Introduction of an AU-rich Element into the 5’ UTR of mRNAs Enhances Protein Expression in Escherichia coli by S1 Protein and Hfq Protein

Lee, Hyang-Mi; Ren, Jun; Kim, Woo Young; Vo, Phuong; Eyun, Seong‐il; Na, Dokyun

doi:10.1007/s12257-020-0348-3

Cited by 6 publications

(1 citation statement)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In E. coli , RPS1 interacts with the 5′UTR of a mRNA and plays an important role in increasing translation efficiency, regardless of the presence of the SD sequence (Komarova et al , 2005 ). RPS1 binds to an AU‐rich sequence upstream of the start codon, and promotes translation initiation by unfolding the mRNA structure (Qu et al , 2012 ; Romilly et al , 2019 ) and protecting the mRNA from degradation, probably by competing against RNase E binding (Lee et al , 2021 ). The lack of RPS1 in Mpn might be one of the reasons why the AU‐content upstream of the start codon was not related to translation efficiency.…”

Section: Discussionmentioning

confidence: 99%

Comprehensive quantitative modeling of translation efficiency in a genome‐reduced bacterium

Weber,

Sogues,

Yus

et al. 2023

Molecular Systems Biology

View full text Add to dashboard Cite

Translation efficiency has been mainly studied by ribosome profiling, which only provides an incomplete picture of translation kinetics. Here, we integrated the absolute quantifications of tRNAs, mRNAs, RNA half‐lives, proteins, and protein half‐lives with ribosome densities and derived the initiation and elongation rates for 475 genes (67% of all genes), 73 with high precision, in the bacterium Mycoplasma pneumoniae (Mpn). We found that, although the initiation rate varied over 160‐fold among genes, most of the known factors had little impact on translation efficiency. Local codon elongation rates could not be fully explained by the adaptation to tRNA abundances, which varied over 100‐fold among tRNA isoacceptors. We provide a comprehensive quantitative view of translation efficiency, which suggests the existence of unidentified mechanisms of translational regulation in Mpn.

show abstract