The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases
We recently demonstrated that the major decapping activity in mammalian cells involves DcpS, a scavenger pyrophosphatase that hydrolyzes the residual cap structure following 3′ to 5′ decay of an mRNA. The association of DcpS with 3′ to 5′ exonuclease exosome components suggests that these two activi...
Saved in:
Published in | The EMBO journal Vol. 21; no. 17; pp. 4699 - 4708 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Chichester, UK
John Wiley & Sons, Ltd
02.09.2002
Blackwell Publishing Ltd Oxford University Press |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | We recently demonstrated that the major decapping activity in mammalian cells involves DcpS, a scavenger pyrophosphatase that hydrolyzes the residual cap structure following 3′ to 5′ decay of an mRNA. The association of DcpS with 3′ to 5′ exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay‐dependent decapping pathway. We purified DcpS from mammalian cells and identified the cDNA encoding a novel 40 kDa protein possessing DcpS activity. Consistent with purified DcpS, the recombinant protein specifically hydrolyzed methylated cap analog but did not hydrolyze unmethylated cap analog nor did it function on intact capped RNA. Sequence alignments of DcpS from different organisms revealed the presence of a conserved hexapeptide, containing a histidine triad (HIT) sequence with three histidines separated by hydrophobic residues. 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. |
---|---|
Bibliography: | ark:/67375/WNG-HTK92GLM-Q istex:3F00B3D1C6480951A4A5050C868DE2FFCA30E24A ArticleID:EMBJ7594667 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
ISSN: | 0261-4189 1460-2075 1460-2075 |
DOI: | 10.1093/emboj/cdf448 |