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higB higB yafQ yafQ yafO yafO relE relE mazF mazF mqsR mqsR prlF prlF yhaV yhaV chpB chpB hicA hicA yoeB yoeB
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higBmRNA interferase toxin of the HigB-HigA toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. A probable translation-dependent mRNA interferase. Overexpression causes cessation of cell growth and inhibits cell proliferation via inhibition of translation; this blockage is overcome by subsequent expression of antitoxin HigA. Overexpression causes cleavage of a number of mRNAs in a translation-dependent fashion, suggesting this is an mRNA interferase. mRNA interferases play a role in bacterial persistence to antibiotics; overexpression of this protein induces p [...] (104 aa)
yafQmRNA interferase toxin of toxin-antitoxin pair YafQ/DinJ; Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific mRNA endoribonuclease that inhibits translation elongation and induces bacterial stasis. Cleavage occurs between the second and third residue of the Lys codon followed by a G or A (5'AAA(G/A)3'), is reading-frame dependent and occurs within the 5' end of most mRNAs. Ribosome-binding confers the sequence specificity and reading frame- dependence. When overexpressed in liquid media YafQ partially inhibits protein synthesis, with a reduction in growth rat [...] (92 aa)
yafOmRNA interferase toxin of the YafO-YafN toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. A translation-dependent mRNA interferase. Overexpression causes cessation of cell growth and inhibits cell proliferation via inhibition of translation; this blockage is overcome by subsequent expression of antitoxin YafN. Overexpression causes cleavage of a number of mRNAs in a ribosome-dependent fashion. YafO binding to the 50S ribosomal subunit in the translation complex induces mRNA cleavage 3' to the region protected by the ribosome; YafO alone is not able to di [...] (132 aa)
relEQin prophage; Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific, ribosome-dependent mRNA endoribonuclease that inhibits translation during amino acid starvation (the stringent response). In vitro acts by cleaving mRNA with high codon specificity in the ribosomal A site between positions 2 and 3. The stop codon UAG is cleaved at a fast rate while UAA and UGA are cleaved with intermediate and slow rates. In vitro mRNA cleavage can also occur in the ribosomal E site after peptide release from peptidyl- tRNA in the P site as well as on free 30S subunits. In vivo [...] (95 aa)
mazFmRNA interferase toxin, antitoxin is MazE; Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific endoribonuclease it inhibits protein synthesis by cleaving mRNA and inducing bacterial stasis. It is stable, single- strand specific with mRNA cleavage independent of the ribosome, although translation enhances cleavage for some mRNAs. Cleavage occurs at the 5'-end of ACA sequences, yielding a 2',3'-cyclic phosphate and a free 5'-OH, although cleavage can also occur on the 3'-end of the first A. Digests 16S rRNA in vivo 43 nts upstream of the C- terminus; this remove [...] (111 aa)
mqsRGCU-specific mRNA interferase toxin of the MqsR-MqsA toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. Plays a significant role in the control of biofilm formation and induction of persister cells in the presence of antibiotics. An mRNA interferase which has been reported to be translation-independent. It has also been reported to be translation-dependent. Cleavage has been reported to occur on either side of G in the sequence GCU. Also reported to cleave after C in GC(A/U) sequences. There are only 14 genes in E.coli W3110 (and probably also MG1655) tha [...] (98 aa)
prlFAntitoxin of the SohA(PrlF)-YhaV toxin-antitoxin system; Antitoxin component of a type II toxin-antitoxin (TA) system. Labile antitoxin that binds to the YhaV toxin and neutralizes its ribonuclease activity. Also acts as a transcription factor. The YhaV/PrlF complex binds the prlF-yhaV operon, probably negatively regulating its expression. (111 aa)
yhaVToxin of the SohB(PrlF)-YhaV toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. Has RNase activity in vitro. Overexpression leads to growth arrest after 30 minutes; these effects are overcome by concomitant expression of antitoxin SohA (PrlF). Massive overexpression is toxic. Unlike most other characterized TA systems degrades rRNA, and co-folding of the both TA proteins is necessary in vitro for inhibition of the RNase activity. It is not known if it has any sequence-specificity. Acts as a transcription factor. The YhaV/PrlF complex binds the prlF-yhaV o [...] (154 aa)
chpBToxin of the ChpB-ChpS toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. ChpB is a sequence-specific mRNA and (weak) tmRNA endoribonuclease that inhibits protein synthesis and induces bacterial stasis. Cleavage is independent of the ribosome. Cleavage occurs at ACY sequences where Y is not C. The endoribonuclease activity is not as strong as that of MazF. The endoribonuclease activity (a toxin) is inhibited by its labile cognate antitoxin ChpS. Toxicity results when the levels of ChpS decrease in the cell, leading to mRNA degradation. Both ChpS and ChpB [...] (116 aa)
hicAmRNA interferase toxin of the HicAB toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. A probable translation-independent mRNA interferase. Overexpression causes cessation of cell growth and inhibits cell proliferation via inhibition of translation; this blockage is overcome (after 90 minutes) by subsequent expression of antitoxin HicB. Overexpression causes cleavage of a number of mRNAs and tmRNA, in a translation-independent fashion, suggesting this is an mRNA interferase. mRNA interferases play a role in bacterial persistence to antibiotics ; Belongs t [...] (58 aa)
yoeBToxin of the YoeB-YefM toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. Its mode of function is controversial; it has been proposed to be an mRNA interferase but also an inhibitor of translation initiation. When overproduced in wild-type cells, inhibits bacterial growth and translation by cleavage of mRNA molecules while it has a weak effect on colony forming ability. Overproduction of Lon protease specifically activates YoeB-dependent mRNA cleavage, leading to lethality. YefM binds to the promoter region of the yefM-yeoB operon to repress transcription [...] (84 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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