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Catalytic processes in addition to the catalytic and noncatalytic forms of the Aa-RNase III–dsRNA structures revealed possible intermediate states of dsRNA binding and a hypothetical pathway of RNase III in vivo. The RNA-free RNase III dimer in conformation A (Figure a, PDB 1O0W) first binds a dsRNA with one of the two dsRBDs. The resulting complex may have at least two possible conformations, B (Figure b, PDB1YZ9 AaRNase IIIE110Q) and E (Figure e, PDB 1YYO), in which the dsRNA is located outside of the catalytic valley. These two conformations, b and e, appear to be interchangeable. In conformation E, the two dsRBDs pack against each other, hindering free rotation of the dsRBD-dsRNA complex around the flexible linker between the endoND and dsRBD. Conformation b allows free rotation of dsRBD-dsRNA around the linker (Figure b). The clockwise rotation of dsRBD-dsRNA leads to the catalytic form (Figure d, PDB 2EZ6) via conformation C (Figure c, PDB 1YYW). Conformations B and C are also likely to be interchangeable. In contrast, a factor that uncouples binding and processing can further stabilize conformation E leading to the noncatalytic form of RNase III (Figure f, PDB 1RC7)[<ref>Blaszczyk, J., et al., Noncatalytic assembly of ribonuclease III with double-stranded RNA. Structure, 2004. 12(3): p. 457-466</ref>, <ref>Gan, J., et al., Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III. Cell, 2006. 124(2): p. 355-66</ref>, <ref>Gan, J., et al., Intermediate states of ribonuclease III in complex with double-stranded RNA. Structure, 2005. 13(10): p. 1435-1442.</ref>].
Catalytic processes in addition to the catalytic and noncatalytic forms of the Aa-RNase III–dsRNA structures revealed possible intermediate states of dsRNA binding and a hypothetical pathway of RNase III in vivo. The RNA-free RNase III dimer in conformation A (Figure a, PDB 1O0W) first binds a dsRNA with one of the two dsRBDs. The resulting complex may have at least two possible conformations, B (Figure b, PDB1YZ9 AaRNase IIIE110Q) and E (Figure e, PDB 1YYO), in which the dsRNA is located outside of the catalytic valley. These two conformations, b and e, appear to be interchangeable. In conformation E, the two dsRBDs pack against each other, hindering free rotation of the dsRBD-dsRNA complex around the flexible linker between the endoND and dsRBD. Conformation b allows free rotation of dsRBD-dsRNA around the linker (Figure b). The clockwise rotation of dsRBD-dsRNA leads to the catalytic form (Figure d, PDB 2EZ6) via conformation C (Figure c, PDB 1YYW). Conformations B and C are also likely to be interchangeable. In contrast, a factor that uncouples binding and processing can further stabilize conformation E leading to the noncatalytic form of RNase III (Figure f, PDB 1RC7)[<ref>Blaszczyk, J., et al., Noncatalytic assembly of ribonuclease III with double-stranded RNA. Structure, 2004. 12(3): p. 457-466</ref>, <ref>Gan, J., et al., Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III. Cell, 2006. 124(2): p. 355-66</ref>, <ref>Gan, J., et al., Intermediate states of ribonuclease III in complex with double-stranded RNA. Structure, 2005. 13(10): p. 1435-1442.</ref>].
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[[Image: Ge470405.f7.gif|thumb|right|420px|Fig.2. ''Hypothetical Pathway Leading to the two Functional Forms of RNase III'' ]]]
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 
</StructureSection>
</StructureSection>
== References ==
== References ==
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<references/>

Revision as of 15:37, 22 April 2015

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Endoribonuclease III

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References

  1. ↑ Lioliou E, Sharma CM, Caldelari I, et al. Global Regulatory Functions of the Staphylococcus aureus Endoribonuclease III in Gene Expression. Hughes D, ed. PLoS Genetics. 2012;8(6):e1002782. doi:10.1371/journal.pgen.1002782
  2. ↑ Lamontagne, B., et al., The RNase III family: a conserved structure and expanding functions in eukaryotic dsRNA metabolism. Yeast, 2001. 45(191): p. 154-158.
  3. ↑ Robertson, H.D., Escherichia coli ribonuclease III cleavage sites. Cell, 1982. 30(3): p. 669-672.
  4. ↑ Grunberg-Manago, M., Messenger RNA stability and its role in control of gene expression in bacteria and phages. Annual review of genetics, 1999. 33(1): p. 193-227.
  5. ↑ Blaszczyk, J., et al., Noncatalytic assembly of ribonuclease III with double-stranded RNA. Structure, 2004. 12(3): p. 457-466.
  6. ↑ Blaszczyk, J., et al., Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage. Structure, 2001. 9(12): p. 1225-1236
  7. ↑ Gan, J., et al., Intermediate states of ribonuclease III in complex with double-stranded RNA. Structure, 2005. 13(10): p. 1435-1442.
  8. ↑ Blaszczyk, J., et al., Noncatalytic assembly of ribonuclease III with double-stranded RNA. Structure, 2004. 12(3): p. 457-466
  9. ↑ Gan, J., et al., Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III. Cell, 2006. 124(2): p. 355-66
  10. ↑ Gan, J., et al., Intermediate states of ribonuclease III in complex with double-stranded RNA. Structure, 2005. 13(10): p. 1435-1442.
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