title: Removal of 5'-terminal m7G from eukaryotic mRNAs by potato nucleotide pyrophosphatase and its effect on translation.
abstract: The procedure for isolation of nucleotide pyrophosphatase (E.C. 3.6.1.9.) from potato has been modified to yield an endonuclease-free preparation purified 2300-fold. The enzyme was used for specific cleavage of pyrophosphate linkages in the 5'-terminal cap (m7GpppN) of several eukaryotic messenger RNAs. Enzymatic removal of 5'-terminal pm7G from reovirus, rabbit globin and Artemia salina mRNAs resulted in an almost complete loss (greater than 80%) of their template activities in a cell-free protein synthesizing system from wheat germ. Incubation with nucleotide pyrophosphatase did not decrease the translation of phage f2 RNA in an Escherichia coli cell-free system.
mesh_terms: D000818:Animals; D006147:Guanine / Q000031:analogs & derivatives*; D007700:Kinetics; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology*; D014176:Protein Biosynthesis; D011755:Pyrophosphatases / Q000302:isolation & purification / Q000378:metabolism*; D012333:RNA, Messenger / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D012333:RNA, Messenger; D006147:Guanine; D011755:Pyrophosphatases