[The C-terminus of transcription factor TnrA from Bacillus subtilis controls DNA-binding domain activity but is not required for dimerization].

Autor: Fedorova KP, Sharafutdinov IS, Turbina EIu, Bogachev MI, Il'inskaia ON, Kaiumov AR
Jazyk: ruština
Zdroj: Molekuliarnaia biologiia [Mol Biol (Mosk)] 2013 Mar-Apr; Vol. 47 (2), pp. 331-7.
DOI: 10.7868/s0026898413020055
Abstrakt: The transcription factor ThrA, which belongs to the MerR transcription regulators, in Bacillus subtilis cells controls genes of nitrogen metabolism under conditions of nitrogen limitation. As all the DNA-binding proteins, it is present as a dimer in cells, but the dimerization site is still unknown. The multiple alignment of TnrA homologs from the other Bacilli allowed to identify the putative dimerization sites. Using the C-terminal truncated TnrA proteins it is established, that, in contrast to other MerR-proteins, the TnrA C-terminus does not participate in dimerization. The surface plasmon resonance has revealed that C-terminus truncations of TnrA do not inactivate its DNA-binding activity. By contrary, it increased an affinity to DNA, confirming that C-terminus controls the DNA-binding activity in a full-length TnrA.
Databáze: MEDLINE