Exoribonuclease from Saccharomyces cerevisiae: effect of modifications of 5' end groups on the hydrolysis of substrates to 5' mononucleotides
Journal Article
·
· Biochem. Biophys. Res. Commun.; (United States)
Using poly(A) as a substrate, an exoribonuclease has been purified from the high-salt wash of ribosomes of Saccharomyces cerevisiae. The product of the reaction of the exoribonuclease is 5' AMP. Hydrolysis of (/sup 3/H)(pA)/sub 3/(/sup 14/C)(pA)/sub n/ shows that both labels are released at the same rate, suggesting that the enzyme acts in a processive manner. Removal of the terminal phosphate of poly(A) with alkaline phosphatase reduces the rate of hydrolysis by 80%. Treatment of the terminally dephosphorylated poly(A) with polynucleotide kinase restores the activity. Two 5' capped mRNA's have been tested and they are hydrolyzed slowly, if at all, by the enzyme. In contrast, phage T4 mRNA, ribosomal RNA, and encephalomyocarditis viral RNA are hydrolyzed at greater than 50% of the rate of poly(A).
- Research Organization:
- Oak Ridge National Lab., TN
- OSTI ID:
- 6850984
- Journal Information:
- Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 81:2; ISSN BBRCA
- Country of Publication:
- United States
- Language:
- English
Similar Records
Exoribonuclease from Saccharomyces cerevisiae: effect of modifications of 5' end groups on the hydrolysis of substrates to 5' mononucleotides
Purification and characterization of a Saccharomyces cerevisiae exoribonuclease which yields 5'-mononucleotides by a 5'. -->. 3' mode of hydrolysis
Evidence for a 5'. -->. 3' direction of hydrolysis by a 5' mononucleotide-producing exoribonuclease from Saccharomyces cerevisiae
Journal Article
·
Wed Mar 29 23:00:00 EST 1978
· Biochem. Biophys. Res. Commun.; (United States)
·
OSTI ID:6550273
Purification and characterization of a Saccharomyces cerevisiae exoribonuclease which yields 5'-mononucleotides by a 5'. -->. 3' mode of hydrolysis
Journal Article
·
Wed Apr 09 23:00:00 EST 1980
· J. Biol. Chem.; (United States)
·
OSTI ID:5308498
Evidence for a 5'. -->. 3' direction of hydrolysis by a 5' mononucleotide-producing exoribonuclease from Saccharomyces cerevisiae
Journal Article
·
Sun Dec 31 23:00:00 EST 1978
· Biochem. Biophys. Res. Commun.; (United States)
·
OSTI ID:5127304
Related Subjects
550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ALKALINE PHOSPHATASE
BACTERIOPHAGES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOCHEMICAL REACTION KINETICS
BIOMASS
CARBON 14
CARBON ISOTOPES
CELL CONSTITUENTS
CHEMICAL REACTIONS
DECOMPOSITION
ENERGY SOURCES
ENZYMES
ESTERASES
EVEN-EVEN NUCLEI
FUNGI
HYDROGEN ISOTOPES
HYDROLASES
HYDROLYSIS
ISOTOPES
KINETICS
LABELLED COMPOUNDS
LIGHT NUCLEI
LYSIS
MICROORGANISMS
NUCLEI
NUCLEOTIDES
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANOIDS
OXYGEN COMPOUNDS
PARASITES
PHOSPHATASES
PHOSPHATES
PHOSPHORUS COMPOUNDS
PHOSPHOTRANSFERASES
PLANTS
PURIFICATION
RADIOISOTOPES
REACTION KINETICS
RENEWABLE ENERGY SOURCES
RIBOSOMES
RNA-ASE
SACCHAROMYCES
SACCHAROMYCES CEREVISIAE
SOLVOLYSIS
SUBSTRATES
TRANSFERASES
TRITIUM
VIRUSES
YEARS LIVING RADIOISOTOPES
YEASTS
59 BASIC BIOLOGICAL SCIENCES
ALKALINE PHOSPHATASE
BACTERIOPHAGES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOCHEMICAL REACTION KINETICS
BIOMASS
CARBON 14
CARBON ISOTOPES
CELL CONSTITUENTS
CHEMICAL REACTIONS
DECOMPOSITION
ENERGY SOURCES
ENZYMES
ESTERASES
EVEN-EVEN NUCLEI
FUNGI
HYDROGEN ISOTOPES
HYDROLASES
HYDROLYSIS
ISOTOPES
KINETICS
LABELLED COMPOUNDS
LIGHT NUCLEI
LYSIS
MICROORGANISMS
NUCLEI
NUCLEOTIDES
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANOIDS
OXYGEN COMPOUNDS
PARASITES
PHOSPHATASES
PHOSPHATES
PHOSPHORUS COMPOUNDS
PHOSPHOTRANSFERASES
PLANTS
PURIFICATION
RADIOISOTOPES
REACTION KINETICS
RENEWABLE ENERGY SOURCES
RIBOSOMES
RNA-ASE
SACCHAROMYCES
SACCHAROMYCES CEREVISIAE
SOLVOLYSIS
SUBSTRATES
TRANSFERASES
TRITIUM
VIRUSES
YEARS LIVING RADIOISOTOPES
YEASTS