Codon bias at the 3′-side of the initiation codon is correlated with translation initiation efficiency in Escherichia coli

Stenström, C.Magnus; Jin, Haining; Major, Louise L.; Tate, Warren P.; Isaksson, Leif A.

doi:10.1016/s0378-1119(00)00550-3

Cited by 152 publications

(148 citation statements)

References 30 publications

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“…interior loop and helix (b) are formed in the presence of the introduced AU-rich sequence; in agreement with data from the literature (21,22), the AU-rich sequence enhanced translation initiation.…”

Section: Theoretical Rna Structure Analysissupporting

confidence: 91%

“…Alternatively, the higher GC content, which increased the tendency to form secondary RNA structures, might lead to the decrease in expression ef®ciency (21,22).…”

Section: In Vitro Transcription/translation Of Linear Expression Consmentioning

confidence: 99%

“…Usually, highly expressed Escherichia coli genes have AU-rich codons immediately following the start methionine (21); GC-rich codons at these positions decrease expression rates (22). Pedersen-Lane and coworkers (22) reported that conversion of purine to thymidine bases at codon positions 3, 4 and 5 increased expression up to 25%.…”

Section: Introductionmentioning

confidence: 99%

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RNA stem-loop enhanced expression of previously non-expressible genes

Paulus¹

2004

Nucleic Acids Research

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The key step in bacterial translation is formation of the pre-initiation complex. This requires initial contacts between mRNA, fMet-tRNA and the 30S subunit of the ribosome, steps that limit the initiation of translation. Here we report a method for improving translational initiation, which allows expression of several previously non-expressible genes. This method has potential applications in heterologous protein synthesis and high-throughput expression systems. We introduced a synthetic RNA stem±loop (stem length, 7 bp; DG 0 = ±9.9 kcal/mol)

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Section: Theoretical Rna Structure Analysissupporting

confidence: 91%

“…Alternatively, the higher GC content, which increased the tendency to form secondary RNA structures, might lead to the decrease in expression ef®ciency (21,22).…”

Section: In Vitro Transcription/translation Of Linear Expression Consmentioning

confidence: 99%

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RNA stem-loop enhanced expression of previously non-expressible genes

Paulus¹

2004

Nucleic Acids Research

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“…The Escherichia coli MG1655 wild-type and the CVR infA(IF1) mutant strains [22] were the hosts for the plasmids [23] used in the lacZ and 3A 0 assay systems. The plasmids are derivatives of pCMS40 and pHN113, respectively.…”

Section: Bacterial Strains and Plasmidsmentioning

confidence: 99%

“…It has been shown that the nature of the +2 codon, that follows the initiation codon, markedly influences gene expression [23,26]. However, no explanation for this phenomenon has been formulated yet.…”

Section: Experimental Strategymentioning

confidence: 99%

In vivo involvement of mutated initiation factor IF1 in gene expression control at the translational level

2005

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Edited by Lev KisselevAbstract The influence in vivo of mutated forms of translation initiation factor (IF1) on the expression of the lacZ or 3A 0 reporter genes, with different initiation and/or +2 codons, has been investigated. Reporter gene expression in these infA(IF1) mutants is similar to the wild-type strain. The results do not support the longstanding hypothesis that IF1 could perform discriminatory functions while blocking the aminoacyl-tRNA acceptor site (A-site) of the ribosome. One cold-sensitive IF1 mutant shows a general overexpression, in particular at low temperatures, of both reporter genes at the protein but not mRNA level.

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Coupling between codon usage, translation and protein export in Escherichia coli

Zalucki

Beacham

Jennings

2011

Biotechnology Journal

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Proteins destined for export via the Sec-dependent pathway are synthesized with a short N-terminal signal peptide. A requirement for export is that the proteins are in a translocationally competent state. This is a loosely folded state that allows the protein to pass through the SecYEG apparatus and pass into the periplasm. In order to maintain pre-secretory proteins in an export-competent state, there are many factors that slow the folding of the pre-secretory protein in the cytoplasm. These include cytoplasmic chaperones, such as SecB, and the signal recognition particle, which bind the pre-secretory protein and direct it to the cytoplasmic membrane for export. Recently, evidence has been published that non-optimal codons in the signal sequence are important for a time-critical early event to allow the correct folding of pre-secretory proteins. This review details the recent developments in folding of the signal peptide and the pre-secretory protein.

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Codon bias at the 3′-side of the initiation codon is correlated with translation initiation efficiency in Escherichia coli

Cited by 152 publications

References 30 publications

RNA stem-loop enhanced expression of previously non-expressible genes

RNA stem-loop enhanced expression of previously non-expressible genes

In vivo involvement of mutated initiation factor IF1 in gene expression control at the translational level

Coupling between codon usage, translation and protein export in Escherichia coli

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