I'm working on a bacterial mutant for a protein with 2 catalytic domains (one EAL and one GGDEF) and it seems that the mutant is only impaired for EAL activity. Is it possible ??
It is possible and similar things have been observed before. Presumably in the folded protein the two catalytic domains are independent of each other and the EAL activity is encoded by the distal segment of the gene. The Tn5 insertion probably disrupts the c-terminal domain and would be in the downstream segment of the gene.
HI Cora, my memory of those publications is vague and from about 20 years ago, so just not able to pull up any examples now. But if some come to mind I'll let you know.