Affinity of dinucleotide cap analogues for human decapping scavenger (hDcpS).
Eukaryotic cells utilize scavenger decapping enzymes to degrade cap structure following 3'-5' mRNA decay. Human DcpS recently has been described as a highly specific hydrolase (a member of the HIT family) that catalyses the cleavage of m(7)GpppG and short capped oligoribonucleotides. We have demonstrated here that cap-1 (m(7)GpppGm) is a preferred substrate among several investigated dinucleotide cap analogues m(7)Gp(n)N (n = 3-5, N is a purine or pyrimidine base) and m(7)GMP is always one of the reaction product. Cap analogues containing pyrimidine base instead of guanine or diphosphate chain are resistant to hydrolysis catalyzed by human scavenger. Contrary to the other enzymes of HIT family, hDcpS activity is not stimulated by Mg(2+).
Darzynkiewicz
Zbigniew M
ZM
Department of Biophysics, Institute of Experimental Physics, Warsaw University, 02-089 Warsaw, Poland.
Bojarska
Elzbieta
E
Stepinski
Janusz
J
Jemielity
Jacek
J
Jankowska-Anyszka
Marzena
M
Davis
Richard E
RE
Darzynkiewicz
Edward
E
D015226:Dinucleoside Phosphates / Q000737:chemistry*; D004722:Endoribonucleases / Q000737:chemistry*; D006801:Humans; D006868:Hydrolysis; D012314:RNA Cap Analogs / Q000737:chemistry*; D020871:RNA Stability
D015226:Dinucleoside Phosphates; D012314:RNA Cap Analogs; C062229:7-methyl-diguanosine triphosphate; D004722:Endoribonucleases; C485332:DcpS protein, human