Characterization of two mRNA-rRNA complexes implicated in the initiation of protein biosynthesis

Steitz, J.A.; Steege, D.A.

Journal of Molecular Biology 114(4): 545-558

1977


ISSN/ISBN: 0022-2836
PMID: 335077
DOI: 10.1016/0022-2836(77)90177-2
Accession: 068526511

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Abstract
To further the molecular understanding of the initiation of protein biosynthesis, additional studies on the interaction of the 3' end of Escherichia coli 16 S RNA with RNA were carried out using 2-colicin fragment.cntdot.initiator region complexes. One contains the R17 A protein initiation site (7 intermolecular base-pairs) and the other a ribosome binding site from the PR transcript of bacteriophage .lambda. (9 intermolecular base-pairs). Requirements for the formation of the .lambda. PR.cntdot.colicin fragment complex in vitro are identical to those previously documented for the R17 A site. Comparative thermal denaturation studies of the 2 complexes yield tm values of 32.degree. C and 37.degree. C for the A site and lambda PR region, respectively. This tm difference and partial nuclease digestion studies performed on the A site.cntdot.colicin fragment complex provide strong experimental support for the previously proposed assignment of residues to the intermolecular base-paired region. The significance of the tm values observed for the 2 complexes and the contribution of mRNA.cntdot.rRNA duplex formation to the initiation event occurring on the ribosome are discussed.