Nucleic Acids Research, 1980, Vol. 8, No. 6 1357-1372
© 1980
Articles |
The binding of T4 gene 32 protein to MS2 virus RNA and transfer RNA
Muséum National d'Histoire Naturelle, Laboratoire de Biophysique 61, rue Buffon, 75005 Paris, France
*To whom correspondence should be sent. Present address : Universidad Autonoma. Departamento de Bioquimica, Facultad de Ciencias. Bellaterra. Barcelona (Spain)
Received February 25, 1980. Fluorescence titrations, absorption spectroscopy and stopped-flow techniques were used to study the interaction of T4 coded 32-protein (P32) with MS2 RNA and total tRNA from E. coli under different ionic conditions. It is shown that the amount of MS2 RNA and tRNA secondary structure melted by P 32 varies markedly and reversibly within a range of ionic condtions under which the binding constant of P 32 to single-stranded nucleic acids unable to form stable hairpins remains higher than 108 M1. Kinetic experiments suggest that P 32 dissociates from the MS2 RNA rewinding strand with a similar rate constant as calculated for the dissociation from single-stranded regions. Possible in vivo consequences of these findings are discussed.