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Isolation and characterization of a polynucleotide phosphorylase from Bacillus amyloliquefaciens.
Metadata
Journaljournal of bacteriology3.004Date
1977-May
Type
Journal Article
Volume
1977-May / 130 : 869-76
Author
Erickson RJ , Grosch JC
DoiPMIDMESH
Adenosine Diphosphate
Bacillus
Chromatography, Gel
Chromatography, Ion Exchange
DNA-Directed RNA Polymerases
Hydrogen-Ion Concentration
Magnesium
Polyribonucleotide Nucleotidyltransferase
RNA, Messenger
Rifamycins
Time Factors
Abstract
Bacillus amyloliquefaciens BaM-2 produces large amounts of extracellular enzymes, and the synthesis of these proteins appears to be dependent upon abnormal ribonucleic acid metabolism. A polynucleotide phosphorylase (nucleoside diphosphate:polynucleotide nucleotidyl transferase) was identified, purified, and characterized from this strain. The purification scheme involved cell disruption, phase partitioning, differential (NH4)2SO4 solubilities, agarose gel filtration, and diethylaminoethyl-Sephadex chromatography. The purified enzyme demonstrated the reactions characteristic of polynucleotide phosphorylase: polymerization, phosphorolysis, and inorganic phosphate exchange with the beta-phosphate of a nucleotide diphosphate. The enzyme was apparently primer independent and required a divalent cation. The reactions for the synthesis of the homopolyribonucleotides, (A)n and (G)n, were optimized with respect to pH and divalent cation concentration. The enzyme is sensitive to inhibition by phosphate ion and heparin and is partially inhibited by rifamycin SV and synthetic polynucleotides.
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J Bacterioljournal of bacteriology
Metadata
LocationUnited States
FromAMER SOC MICROBIOLOGY

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