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Enzymatic Complex Summary

DCP1-DCP2 decapping complex from Saccharomyces cerevisiae



Structure of DCP1-DCP2 decapping complex (Saccharomyces cerevisiae):

 
Protein components:
mRNA-decapping enzyme subunit 1
mRNA-decapping enzyme subunit 2
 

 

The decapping enzyme is a dimer that consists of Dcp1 and Dcp2 proteins. Dcp2, which contains a MutT domain, supplies the catalytic activity. 
 
Several accessory factors are required for efficient decapping. First, the Sm-like (Lsm) proteins seem to be
involved in the 5′→3′ mRNA-decay process. The heptameric Lsm1–7 complex associates with the 3′ end of deadenylated mRNAs and promotes decapping. Other Lsm proteins, namely EDC3 (enhancer of decapping-3; also known as Lsm16) and the PABP-binding protein-1 (Pbp1) have been implicated in mRNA turnover. 
 
Additional decapping accessory proteins include the DExD/H-box RNA helicase Dhh1 (also known as RCK/p54 or Me31B) and Pat. Dhh1 and Pat1 have a role in mediating translational repression as well as decapping.
 


Reactions in which DCP1-DCP2 decapping complex is involved:
Pathways in which DCP1-DCP2 decapping complex is involved:
References:

Authors Title Journal
Garneau NL, Wilusz J, Wilusz CJ The highways and byways of mRNA decay. Nat Rev Mol Cell Biol 2007-01-01



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Last modification of this entry: April 27, 2012.

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