Q beta replicase containing a Bacillus stearothermophilus elongation factor.
We purified Q beta replicase containing EF-Ts from Bacillus stearothermophilus in place of the homologous polypeptide from Escherichia coli. The hybrid enzyme was fully active in the transcription of a variety of templates. It was found to be qualitatively similar to native Q beta replicase with respect to a variety of parameters which measure the efficiency of initiation of RNA synthesis. The results demonstrated that Q beta replicase can tolerate substantial alterations in the EF-Tu X Ts component of the enzyme. These alterations resulted in only minor perturbations of catalytic properties.
D004926:Escherichia coli / Q000201:enzymology*; D001411:Geobacillus stearothermophilus / Q000032:analysis; D006153:Guanosine Diphosphate / Q000494:pharmacology; D006160:Guanosine Triphosphate / Q000494:pharmacology; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000032:analysis*; D011777:Q beta Replicase / Q000032:analysis / Q000378:metabolism*; D012316:RNA Nucleotidyltransferases / Q000378:metabolism*; D012367:RNA, Viral / Q000096:biosynthesis*
D010445:Peptide Elongation Factors; C028696:Qbeta ribonucleic acid; D012367:RNA, Viral; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D011777:Q beta Replicase; D012316:RNA Nucleotidyltransferases; D010444:Peptide Elongation Factor Tu