Author: Byszewska, Magdalena; Smietanski, Miroslaw; Purta, Elzbieta; Bujnicki, Janusz M
Title: RNA methyltransferases involved in 5' cap biosynthesis Document date: 2015_1_27
ID: sz2531mv_17
Snippet: Studies of cap composition of human mRNAs conducted in mid-70s revealed that when the first nucleotide of the transcript is an adenosine, this base can be methylated to m 6 A. 8, 71 The enzyme that catalyzes the conversion of m 7 GpppAm ends of mRNA to m 7 Gpppm 6 Am has been isolated from a cytoplasmic fraction of HeLa cells. The isolated enzyme showed no activity toward internal adenosines. 72 Recently, Schwartz and coworkers studied the m 6 A .....
Document: Studies of cap composition of human mRNAs conducted in mid-70s revealed that when the first nucleotide of the transcript is an adenosine, this base can be methylated to m 6 A. 8, 71 The enzyme that catalyzes the conversion of m 7 GpppAm ends of mRNA to m 7 Gpppm 6 Am has been isolated from a cytoplasmic fraction of HeLa cells. The isolated enzyme showed no activity toward internal adenosines. 72 Recently, Schwartz and coworkers studied the m 6 A mRNA methylome following depletion of multiprotein methyltransferase complex components METTL3, METTL14, KIAA1429, and WTAP, and implicated the involvement of the METTL3, METTL14, and KIAA1429 proteins in m 6 A formation at the internal sites but not at the 5 0 sites. 73 The full characterization of the cap-specific m 6 A methyltransferase activity requires further studies in vitro.
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