Template activity of complexes formed between bacteriophage f2 RNA and coat protein.
AUTOR(ES)
Zagórska, L
RESUMO
Formation of complexes between f2 RNA polymerase cistron was partially inhibited, some RNA and coat protein was studied using salt conditions which are optimum for phage protein synthesis. In this ionic environment, coat protein precipitation can be prevented by sulfhydryl group-protecting agents. Complexes formed at different protein-RNA input molar ratios were isolated and tested for template activity in an in vitro protein synthesizing system. Simultaneously, the number of protein molecules bound per RNA strand in such complexes was measured by the membrane (Millipore) filtration technique. Under conditions in which translation of the RNA strands were complexed with six molecules of coat protein, whereas some remained unbound. Strong inhibition of the translation of the RNA polymerase cistron was observed when each of the RNA strands present in the mixture was associated with six molecules of coat protein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=354487Documentos Relacionados
- Specificity of Formation of Complexes Between Coat Protein and Bacteriophage f2 RNA
- Hexamer of bacteriophage f2 coat protein as a repressor of bacteriophage RNA polymerase synthesis.
- The RNA binding site of bacteriophage MS2 coat protein.
- Probing sequence-specific RNA recognition by the bacteriophage MS2 coat protein.
- BIOSYNTHESIS OF THE COAT PROTEIN OF COLIPHAGE f2 BY E. COLI EXTRACTS*