mRNA-decapping enzyme from Saccharomyces cerevisiae: purification and unique specificity for long RNA chains.

Abstract:

:An enzyme that hydrolyzes one PPi bond of the cap structure of mRNA, yielding m7GDP and 5'-p RNA was purified from Saccharomyces cerevisiae to a stage suitable for characterization. The specificity of the enzyme was studied, using both yeast mRNA and synthetic RNAs labeled in the cap structure. A synthetic capped RNA (540 nucleotides) was not reduced in size, while as much as 80% was decapped. Yeast mRNA treated with high concentrations of RNase A, nuclease P1, or micrococcal nuclease was inactive as a substrate. The use of synthetic capped RNAs of different sizes (50 to 540 nucleotides) as substrates showed that the larger RNA can be a better substrate by as much as 10-fold. GpppG-RNA was hydrolyzed at a rate similar to that at which 5'-triphosphate end group were not hydrolyzed.

journal_name

Mol Cell Biol

authors

Stevens A

doi

10.1128/mcb.8.5.2005

subject

Has Abstract

pub_date

1988-05-01 00:00:00

pages

2005-10

issue

5

eissn

0270-7306

issn

1098-5549

journal_volume

8

pub_type

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