Translational repression mechanisms in prokaryotes

Schlax, Paula J.; Worhunsky, David J.

doi:10.1046/j.1365-2958.2003.03517.x

Cited by 54 publications

(50 citation statements)

References 43 publications

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“…It was proposed that the entrapment mechanism would sustain rather weak binding affinities of protein-mRNA complex. 18,19 In agreement with this observation, the binding affinity of EcS15 is about one order of magnitude lower than that for its 16S rRNA binding site and of TtS15 for its mRNA target. In B. stearothermophilus (Fig.…”

Section: Plasticity Of Mrna-regulatory Protein Recognition In Translasupporting

confidence: 73%

The role of mRNA structure in translational control in bacteria

Geissmann¹,

Marzi²,

Romby³

2009

RNA Biology

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Section: Plasticity Of Mrna-regulatory Protein Recognition In Translasupporting

confidence: 73%

The role of mRNA structure in translational control in bacteria

Geissmann¹,

Marzi²,

Romby³

2009

RNA Biology

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“…This indicated that the predicted structural conformation between the two genes prevented amplification of complete cDNA during the reverse transcriptase reaction. The efficiency of translational initiation and regulation is strongly correlated with the structure of the ribosomebinding site (RBS) (Schlax & Worhunsky, 2003). The primary interaction between mRNA and the 30S subunit rRNA requires local single-stranded mRNA (Draper, 1987(Draper, , 1996Gualerzi & Pon, 1990;Draper et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

Characterization of the Bacillus cereus Nhe enterotoxin

et al. 2004

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The non-haemolytic enterotoxin (Nhe) is one of two three-component enterotoxins responsible for the diarrhoeal food-poisoning syndrome caused by Bacillus cereus. Nhe is composed of NheA, NheB and NheC. The three genes encoding the Nhe components constitute an operon, and the transcriptional start site is located 61 bp upstream of the nheA translational start site. The nhe genes were cloned separately, and expressed in either Bacillus subtilis or Escherichia coli. Separate expression showed that all three components were required for biological activity. In addition, NheA and NheB were purified from B. cereus culture supernatants. As NheC seems to be expressed in only small amounts by B. cereus, NheC was expressed and purified as a histidine-tagged fusion protein. The maximum cytotoxic activity was obtained when the molar ratio between NheA : NheB : His 6 -NheC was 10 : 10 : 1, and it was shown that NheB was the binding component of the enterotoxin complex.

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“…The binding of trans-acting proteins and/or antisense RNA to target mRNA can allosterically control translation (reviewed in Ref. 37). As being revealed from our results on hsdA regulation, RepB acts as a trans-acting factor that modulates hsdA expression by repressing 3␣-HSD/CR mRNA translation.…”

Section: Discussionmentioning

confidence: 52%

“…As being revealed from our results on hsdA regulation, RepB acts as a trans-acting factor that modulates hsdA expression by repressing 3␣-HSD/CR mRNA translation. The occurrence of cis-acting mRNA elements in the 3␣-HSD/CR mRNA structure that could repress hsdA translation was additionally excluded by temperature shift experiments of the bacterial cultures from 30 to 42°C (data not shown) (37).…”

Section: Discussionmentioning

confidence: 99%

Identification and Characterization of a Novel Translational Repressor of the Steroid-inducible 3α-Hydroxysteroid Dehydrogenase/Carbonyl Reductase Gene in Comamonas testosteroni

Guan

Martin

Maser

2003

Journal of Biological Chemistry

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Comamonas testosteroni 3␣-hydroxysteroid dehydrogenase/carbonyl reductase (3␣-HSD/CR) is a key enzyme in the degradation of steroid compounds in soil and may therefore play a significant role in the bioremediation of hormonally active compounds in the environment. The enzyme is also involved in the degradation of the steroid antibiotic fusidic acid. In addition, 3␣-HSD/CR mediates the carbonyl reduction of non-steroidal aldehydes and ketones. Because the gene of 3␣-HSD/CR (hsdA) is inducible by steroids, we were interested in the mode of its molecular regulation. Recently, we could identify the first molecular determinant in procaryotic steroid signaling, i.e. a repressor protein (RepA), which acts as a negative regulator by binding to upstream operator sequences of hsdA, thereby blocking hsdA transcription. In this work, we identified and cloned a second novel regulator gene that we named repB. The gene locates 932 bp downstream from hsdA on the C. testosteroni chromosome with an orientation opposite to that of hsdA. The open reading frame of repB consists of 237 bp and translates into a protein of 78 amino acids that was found to act as a repressor that regulates hsdA expression on the translational level. Northern blot analysis, UV-cross linking, gel-shift assays, and competition experiments proved that RepB binds to a 16-nucleotide sequence downstream of AUG at the 5 end of the 3␣-HSD/CR mRNA, thereby blocking hsdA translation. Testosterone, on the other hand, was shown to specifically bind to RepB, thereby yielding the release of RepB from the 3␣-HSD/CR mRNA such that hsdA translation could proceed. Data bank searches with the RepB primary structure yielded a 46.2% identity to the regulator of nucleoside diphosphate kinase, a formerly unknown protein from Escherichia coli that can restore a growth defect in alginate production in Pseudomonas aeruginosa. In conclusion, the induction of hsdA by steroids in fact is a derepression where steroidal inducers bind to two repressor proteins, RepA and RepB, thereby preventing blocking of hsdA transcription and translation, respectively.

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Translational repression mechanisms in prokaryotes

Cited by 54 publications

References 43 publications

The role of mRNA structure in translational control in bacteria

The role of mRNA structure in translational control in bacteria

Characterization of the Bacillus cereus Nhe enterotoxin

Identification and Characterization of a Novel Translational Repressor of the Steroid-inducible 3α-Hydroxysteroid Dehydrogenase/Carbonyl Reductase Gene in Comamonas testosteroni

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