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Contest ends March 20th, 10AM ET. Winner will be emailed and announced via FB and email, then that person will have 48hrs to respond.Mutations inducing the premature termination of bacterial transcription. Effects on DNA melting and DNA-protein interactions.
The effects of premature termination of RNA polymerase transcription on the structure and stability of DNA were investigated (pB6, pM10, pE1, and pE2) in vitro by using an in vitro transcription system which faithfully mimics transcription in vivo. We compared two types of premature termination mutations, UAG and UAA, causing production of a truncated leader peptide and termination of RNA chain elongation at codons UAG, at UAA or at the two codons simultaneously. The temperature dependent DNase I specific cleavage of the DNA in mutant pB6, and DNA-protein interactions in the pB6 DNA was studied. The following results were obtained. (i) The DNA strands of the three mutant pB6 DNAs (UAG, UAA and both UAG and UAA) are relatively destabilized, as indicated by increase of the melting temperature for DNA-bound proteins, by increase of the Tm of the free DNA and by increase of the DNase I temperature at which half of the substrate is cleaved. (ii) The increase in Tm for protein associated DNA is correlated with the position of the termination site, UAG being the most destabilizing nucleotide and UAA the least destabilizing nucleotide, indicating that they induce more stable protein-DNA complexes. (iii) This destabilization of DNA-protein complexes appears not to be related to structural features of the UAG and UAA codons. The changes of Tm for protein associated DNA and of DNase I specific cleavage appear to be independent of each other.Q:
How to get the current selected value after post-back
shows an example