The competence transcription factor ComK is the master regulator of competence development in Bacillus subtilis. In the regulatory pathway, ComK is involved in different interactions: (i) protein-DNA interactions to stimulate transcription of ComK-dependent genes and (ii) protein-protein interactions, divided into interactions with other proteins and interactions between ComK proteins involving oligomerization. The fact that ComK displays different types of interactions suggests the presence of

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... specific, distinct domains in the protein. This paper describes a search for functional domains, by constructing ComK truncation variants, which were tested for DNA binding, oligomerization and transcription activation. Truncations at the C-terminal end of ComK demonstrated the requirement of this part for transcription activation, but not for DNA binding. The C-terminal region is probably involved in oligomerization of ComK-dimers into tetramers. Surprisingly, a ComK truncation variant lacking 9 aa from the N-terminal end (DN9ComK) showed higher transcription activation than wild-type ComK, when expressed in Lactococcus lactis. However, in B. subtilis, transcription activation by DN9ComK was twofold lower than that by wild-type ComK, resulting from a five-to sixfold lower protein level of ComKDN9. Thus, relatively, DN9ComK is more active in transcription activation than wild-type ComK. These results suggest that the presence of this N-terminal extension on ComK is a trade-off between high transcription activation and a thus far unidentified role in regulation of ComK.