Specificity of a nucleolar 2'-O-methyltransferase for RNA substrates.

Abstract

In this study we examined the specificity of a nucleolar 2'-O-methyltransferase isolated from nucleoli of Ehrlich ascites tumor cells. The nucleolar methyltransferase was capable of methylating each of the four nucleosides of RNA, however, the level of methylation at a particular nucleoside varied with the type of RNA. Both kinetic analysis and the stimulation of methylation by polyamines suggested that the structure of RNA was critical in influencing the discrimination and apparent specificity of nucleolar 2'-O-methyltransferase.

• Authors: D C Eichler, S J Eales
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 155 Issue 1 Pg. 530-7 (Aug 30 1988) ISSN: 0006-291X [Print] United States
• PMID: 3415705 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Guanosine
• Cytosine
• Methyltransferases
• RNA 2'-O-methyltransferase
• Adenosine
• Uridine

Topics

• Adenosine (metabolism)
• Animals
• Carcinoma, Ehrlich Tumor (enzymology, genetics)
• Cell Nucleolus (enzymology)
• Cytosine (metabolism)
• Guanosine (metabolism)
• Kinetics
• Methyltransferases (metabolism)
• Mice
• Structure-Activity Relationship
• Substrate Specificity
• Uridine (metabolism)