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JBC, Vol. 251, Issue 7, 1902-1912, Apr, 1976
A. W. Senear and J. A. Steitz
We have studied the interaction of the host factor (HF) required for
bacteriophage Qbeta RNA replication and of ribosomal protein S1, a subunit
of Qbeta replicase, with Qbeta and R17 RNA. Both proteins bind to both
Qbeta and R17 RNA; HF has a higher affinity than S1 for these phages RNAs.
HF binds to a single site in R17 RNA located in the replicase cistron, and
to two sites of Qbeta RNA, one of which is located approximately 60
nucleotides from the 6' end of Qbeta RNA. The three HF binding sites all
have portions rich in adenylate residues; all are bound by HF when
contained in oligonucleotides which are predicted to exist only in
single-stranded form. S1 selects a single site in Qbeta RNA, also near the
6' end, but binds to a large number of sites in R17 RNA. These results
suggest that HF and possibly S1, through their interaction with the
3'-terminal region of Qbeta RNA, are directly involved in the recognition
of the 6' end of Qbeta RNA by Qbeta replicase. Under conditions where
specific protein-R1M RNA complexes are formed, we have also tested host
factor and S1 for cistron-specific interference with ribosome binding to
R17 RNA. Although S1 and HF lower the efficiency of initiation complex
formation as described previously, we detect no discrimination against any
particular cistron. We therefore conclude that translational interference
exhibited by the two proteins probably reflects simply their high affinity
for RNA and certain defined polynucleotides.
Site-specific interaction of Qbeta host factor and ribosomal protein S1 with Qbeta and R17 bacteriophage RNAs
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