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Multiple Nudix family proteins possess mRNA decapping activity
Man-Gen Song1, Sophie Bail, Megerditch Kiledjian
1Department of Cell Biology and Neuroscience, Rutgers University, Piscataway, New Jersey 08854-8082, USA.
RNA (New York, N.Y.)
|January 29, 2013
Summary
Multiple Nudix hydrolase family members exhibit RNA decapping activity, expanding the known enzymes involved in mRNA decay and gene expression regulation across species.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- RNA decapping is crucial for gene expression and mRNA decay.
- Mammalian cells have at least two known decapping enzymes, Dcp2 and Nudt16.
- Both known enzymes belong to the Nudix hydrolase family.
Purpose of the Study:
- To investigate if other Nudix hydrolase family members possess RNA decapping activity.
- To characterize the decapping activity of additional Nudix proteins.
Main Methods:
- In vitro assays were used to test the decapping activity of six mouse Nudix proteins.
- Analysis of decapping products (m⁷GDP, m⁷GMP) was performed.
- Saccharomyces cerevisiae and bacterial Nudix proteins were also investigated.
Main Results:
- Six additional mouse Nudix proteins (Nudt2, Nudt3, Nudt12, Nudt15, Nudt17, Nudt19) showed varying decapping activity.
- Nudt17 and Nudt19 produced m⁷GDP, similar to Dcp2.
- Nudt2, Nudt3, Nudt12, and Nudt15 produced both m⁷GMP and m⁷GDP.
- All tested Nudix proteins could decapped unmethylated capped RNA.
- Yeast Ddp1p and bacterial RppH also exhibited decapping activity.
Conclusions:
- Multiple Nudix family hydrolases possess intrinsic RNA decapping activity.
- RNA decapping is an evolutionarily conserved function.
- These findings broaden the understanding of enzymes involved in mRNA stability and gene regulation.
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