Sandbox reserved 330: Difference between revisions

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{{STRUCTURE_1ne8| PDB=1ne8 | SCENE= }}
{{STRUCTURE_1ne8| PDB=1ne8 | SCENE= }}
==Overview of YdcE==
==Overview of YdcE==
The Bacilis subtilis YdcE gene encodes an endoribonuclease called EndoA, which is a member of the MazF/PemK family of bacterial toxin and the protein encoded by the gene YdcD is an inhibitor of its activity. EndoA cleaves in a UAC sequence, which is predicted to be a single stranded conformation, and has an overlapping cleavage site specificity with the E.coli homologues. EndoA activity results in cleavage products with a 3’phosphate and 5’OH group, which is typical of degradative RNAses that functions in the absence of divalent cations <ref > Pellegrini, O., Mathy, N., Gogos.A., Shapiro, L., Condon, C. The Bacillus subtilis YdcDE operon encodes an endoribonuclease of the MazF/PemK family and its inhibitor. Molecular Microbiology.2005. June;56(5):1139-1148</ref>  
The Bacilis subtilis YdcE gene encodes an endoribonuclease called EndoA, which is a member of the MazF/PemK family of bacterial toxin and the protein encoded by the gene YdcD is an inhibitor of its activity. EndoA cleaves at the UAC sequence, which is predicted to be a single stranded conformation, and has an overlapping cleavage site specificity with the E.coli homologues. EndoA activity results in cleavage products with a 3’phosphate and 5’OH group, which is typical of degradative RNAses that functions in the absence of divalent cations <ref > Pellegrini, O., Mathy, N., Gogos.A., Shapiro, L., Condon, C. The Bacillus subtilis YdcDE operon encodes an endoribonuclease of the MazF/PemK family and its inhibitor. Molecular Microbiology.2005. June;56(5):1139-1148</ref>  


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== Toxin and Anti-toxin pair==
== Toxin and Anti-toxin pair==
Addiction modules, consisting of a toxin and antitoxin pair, are controlled by operons which, are autoregulated at the transcriptional level. Bacteria rely on addiction modules to maintain plasmids within populations, and cells that do not inherit the plasmid encoded operon will not produce antixoin and will be inhibited by the toxin via post segregational killing. Once this operon is expressed, the bacterial strain is addicted to the antitoxin for survival. It is known that genomes of most bacteria have a toxin-antitoxin loci, which have been shown to be induced by stressful conditions. So thus, these modules play an important role in plasmid partitioning and cellular response to stress, where the maintenance of these modules prevents the lethal effect of toxin on cells.
Addiction modules, consisting of a toxin and antitoxin pair, are controlled by operons which, are autoregulated at the transcriptional level. Bacteria rely on addiction modules to maintain plasmids within populations, and cells that do not inherit the plasmid encoded operon will not produce antixoin and will be inhibited by the toxin via post segregational killing. Once this operon is expressed, the bacterial strain is addicted to the antitoxin for survival. It is known that genomes of most bacteria have a toxin-antitoxin loci, which have been shown to be induced by stressful conditions<ref name="Pellegrini"/>. So thus, these modules play an important role in plasmid partitioning and cellular response to stress, where the maintenance of these modules prevents the lethal effect of toxin on cells.


Previous studies of toxin families include MazF, ChpAK, and PemK, which all code for endoribonuclease that activates cellular mRNAs by cleaving them at specific sites.  Recently, there is a Bacilis subtilis gene product discovered, EndoA, that is a member of RNAses, which is likely the gene product of the YdcE gene. This EndoA has similar cleavage pattern specificity as MazF and PemK, with cleavage products of a 3’phosphate and 5’OH group. Further study revealed that a coexpression of an upstream gene, YdcD reverses the effects of this particular toxin, and thus, this is the first antitoxin-toxin system of Bacilis subtilis.  
Previous studies of toxin families include MazF, ChpAK, and PemK, which all code for endoribonuclease that activates cellular mRNAs by cleaving them at specific sites.  Recently, there is a Bacilis subtilis gene product discovered, EndoA, that is a member of RNAses, which is likely the gene product of the YdcE gene. This EndoA has similar cleavage pattern specificity as MazF and PemK, with cleavage products of a 3’phosphate and 5’OH group. Further study revealed that a coexpression of an upstream gene, YdcD reverses the effects of this particular toxin, and thus, this is the first antitoxin-toxin system of Bacilis subtilis.