The Interaction of RNase M5 with a 5S rRNA Precursor

Abstract

As is evident from several other papers in this volume, considerable information regarding the posttranscriptional processing of tRNA is accumulating. Although most RNA molecules, in both prokaryotes and eukaryotes, are the products of more or less extensive posttranscriptional metabolism, detailed studies of these processes have been possible only with tRNA and 5S rRNA of Bacillus subtilis. Although not directly involved with tRNA, studies of the processing of 5S rRNA are relevant in this area of study in that much of this methodology is immediately applicable to the study of the maturation of the precursors of tRNA. Moreover, there is the common goal of understanding the nature of protein-polynucleotide interactions. In brief, we have isolated the endonuclease responsible for the terminal maturation of 5S rRNA in B. subtilis and devised procedures for altering the precursor RNA substrate to explore the polynucleotide recognition elements utilized by this highly specific enzyme.

THE MATURATION OFB. SUBTILIS 5S rRNA
Because of its simple structure (about 120 nucleotides long), 5S rRNA is useful for exploring the details of posttranscriptional RNA metabolism. At the outset of these studies, we felt that the 5S rRNA of Escherichia coli was not likely to be a suitable model, since the immediate precursor of 5S rRNA in this organism is maximally only 3 nucleotides larger than the mature form (Monier et al. 1970) and such limited precursor-specific length might not be of functional significance. We therefore undertook a search for an organism utilizing more complex 5S rRNA metabolism than that...