Crystal structures of human DcpS in ligand-free and m7GDP-bound forms suggest a dynamic mechanism for scavenger mRNA decapping.

@article{Chen2005CrystalSO,
  title={Crystal structures of human DcpS in ligand-free and m7GDP-bound forms suggest a dynamic mechanism for scavenger mRNA decapping.},
  author={Nan Chen and Martin A. Walsh and Yuying Liu and Roy Parker and Haiwei Song},
  journal={Journal of molecular biology},
  year={2005},
  volume={347 4},
  pages={
          707-18
        }
}

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References

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The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases
TLDR
Mutagenesis analysis revealed that the central histidine within the DCPS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function.
Functional analysis of mRNA scavenger decapping enzymes.
TLDR
A functional characterization of the DCPS enzyme is carried out and it is demonstrated that unlike previously described HIT proteins, DcpS is a modular protein that requires both the core HIT fold at the carboxyl-terminal and sequences at the amino-terminus of the protein for cap binding and hydrolysis.
Functional characterization of the mammalian mRNA decapping enzyme hDcp2.
TLDR
It is demonstrated that hDcp2 is an RNA-binding protein and its recognition and hydrolysis of the cap substrate is dependent on an initial interaction with the RNA moiety.
The hDcp2 protein is a mammalian mRNA decapping enzyme
TLDR
The mammalian homologue of the yeast Dcp2 protein is an mRNA decapping enzyme demonstrated to contain intrinsic decapping activity, yet unlike yeast, competition of cap-binding proteins by cap analog did not influence the efficiency of decapping.
Analysis of recombinant yeast decapping enzyme.
TLDR
These experiments demonstrate that copurification of Dcp1p and Dcp2p yields active decapping enzyme under a variety of conditions, and can reconstitute the activation of decapping with recombinant proteins, which indicates that the Edc1 and Edc2 proteins act directly on the decapping enzymes.
Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures
TLDR
It is shown that recombinant human Dcp2 (hDCP2) is enzymatically active and appears evolutionarily conserved, and Mutational and biochemical analyses indicate that the hDcp2 MutT/Nudix domain mediates this activity.
The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif
TLDR
Results suggest that direct or indirect interaction of Dcp1p with Dcp2p is required for the production of active decapping enzyme, perhaps in a process requiring the hydrolysis of a pyrophosphate bond.
Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit.
TLDR
Evidence is presented that His-96 --> Asn protein binds ApppA well and forms an enzyme-AMP intermediate extremely poorly, suggesting that Fhit-substrate complexes are the likely signaling form of the enzyme.
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