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

Journal Article · Sun May 01 04:00:00 EDT 1988 · Mol. Cell. Biol.; (United States)

DOI:https://doi.org/10.1128/MCB.8.5.2005· OSTI ID:7192107

Stevens, A

An enzyme that hydrolyzes one PP/sub i/ bond of the cap structure of mRNA, yielding m/sup 7/GDP 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 m/sup 7/GpppG-RNA was hydrolyzed. The PP/sub i/ bonds of an RNa containing a 5'-triphosphate end group were not hydrolyzed.

• Research Organization: Biology Div., Oak Ridge National Lab., Oak Ridge, TN (US)
• OSTI ID: 7192107
• Journal Information: Mol. Cell. Biol.; (United States), Journal Name: Mol. Cell. Biol.; (United States) Vol. 8:5; ISSN MCEBD
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BIOCHEMICAL REACTION KINETICS
CHEMICAL REACTIONS
DECOMPOSITION
DNA-ASE
ENDONUCLEASES
ENZYMATIC HYDROLYSIS
ENZYME REACTIVATION
ENZYMES
ESTERASES
FUNGI
HYDROLASES
HYDROLYSIS
KINETICS
LABELLING
LYSIS
MESSENGER-RNA
MICROORGANISMS
NUCLEIC ACIDS
NUCLEOTIDYLTRANSFERASES
ORGANIC COMPOUNDS
PHOSPHODIESTERASES
PHOSPHORUS-GROUP TRANSFERASES
PLANTS
POLYMERASES
PURIFICATION
REACTION KINETICS
RNA
RNA POLYMERASES
RNA-ASE
SACCHAROMYCES
SACCHAROMYCES CEREVISIAE
SOLVOLYSIS
SPECIFICITY
TRANSFERASES
YEASTS