Wilming, MartinJohnsson, Kai2006-02-272006-02-272006-02-27200110.1016/S0014-5793(01)03179-9https://infoscience.epfl.ch/handle/20.500.14299/226631WOS:00017275750002528The inter- and intramol. interactions between the different domains of the catalase-peroxidase KatG from Mycobacterium tuberculosis were analyzed using the two-hybrid assay. It was shown that the dimerization of the enzyme is due to a strong interaction of the first 99 amino acids of the N-terminal domain whereas the C-terminal domain does not play a role in the dimerization. In addn., an intramol. interaction between the N- and C-terminal domains was detected which might play a functional role in the mechanism of the enzyme. [on SciFinder (R)]text::journal::journal article::research article