Sandbox reserved 330: Difference between revisions

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{{STRUCTURE_1ne8| PDB=1ne8 | SCENE= }}
{{STRUCTURE_1ne8| PDB=1ne8 | SCENE= }}
==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.
 
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== Background Information==
== 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. 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.   


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The active site of the YdcE protein is composed of residues from both monomers, with key active site residues consisting of Pro1, Arg 11, Arg 38, Phe50. Dimerization of the two monomers include Pro1, which is presumed to be the catalytic base and is from one subunit, while Phe8, Arg 10, Trp 51, and Tyr72 are from the other monomer.  
The active site of the YdcE protein is composed of residues from both monomers, with key active site residues consisting of Pro1, Arg 11, Arg 38, Phe50. Dimerization of the two monomers include Pro1, which is presumed to be the catalytic base and is from one subunit, while Phe8, Arg 10, Trp 51, and Tyr72 are from the other monomer.  
==Conclusion==
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>PMID:14517982</ref>
<ref>PMID:14517982</ref>
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<references/>
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