The tRNA function of SsrA contributes to controlling repression of bacteriophage Mu prophage

The small regulatory RNA SsrA has both tRNA and mRNA activities. It charges alanine and interacts with stalled ribosomes, allowing for translation to resume on the SsrA mRNA moiety. Hence, unfinished peptides carry a short am ino acid tag, which serves as a signal for degradation by energy-dependent proteases. In SsrA-defective Escherichia coli strains, thermoinducible muta nts of the transposable bacteriophage Mu (Mucts) are no longer induced at h igh temperature. Here we show that truncated forms of the key regulator of Mu lysogeny, the repressor Repc, accumulate in the absence of SsrA. These f orms resemble C-terminally truncated dominant Mu repressor mutants previous ly isolated from Mucts, which are no longer thermoinducible and bind operat or DNA with a high affinity even at high temperature. Using various ssrA al leles, we demonstrate the importance of SsrA charging on the ribosome for c ontrolling Mu prophage repression. Our results thus substantiate the previo us observation that trans-translation is not the only function of the SsrA. The alternative function of SsrA appears to influence the stability of Mu lysogens by controlling the translation of the C-terminal domain of the rep ressor protein, which modulates the affinity of the protein for DNA and its susceptibility to proteolytic degradation.