IGERT NIMBIOS NSF
 
The mystery of the enolase pocket
 
 
Authors          Audiences          Overview           Materials          Resources           Future Directions
 

 


Authors


Joseph McCray
Morehouse College


Kathy Takayama
Brown University

 
   
 


Brief Overview:

In bacteria, enolase binds to the non-catalytic domain of RNase E and has been implicated in modulating RNase E activity under certain conditions. We have investigated the structural correlates of the enolase binding region (which is separate from the catalytic site).  

 
   
 


Project Materials:

Swiss PDB viewer PDB Genbank  

 
 


Resources and References:

Morita et al. (2004) Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli. Mol. Micro. 54(4):1063-1075 Vanzo, N.F., Li, Y.S., Py, B., Blum, E., Higgins, C.F., Raynal, L.C., et al. (1998) Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome. Genes Dev 12: 2770–2781. Chandran & Luisi (2006) Recognition of enolase in the Escherichia coli RNA degradosome. J. Mol. Biol. 358:8–15. Callaghan et al. (2004) Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. J. Mol. Biol. 340:965–979. Erce et al. (2009) Identification and functional analysis of RNase E of Vibrio angustum S14 and two-hybrid analysis of its interaction partners. Biochimica et Biophysica Acta 1794:1107–1114  

 
   
 


Future Directions:

Comparisons of more species as structures become available Molecular dynamic modeling and simulation of interaction of enolase with RNase E simultaneously with RNase E catalytic function.  

 
 


Attachments


- Takayama_McCrayv2.ppt