Some proteins need additional processing to become fully functional, for example NiFe-hydrogenases need to be cleaved by endopeptidases for some of their subunits to be active.
Is it known whether transcription regulators could also, in some cases, need such extensive post-translational modification to be effective?
(I am not talking about possible conformational changes that by specific effectors, but rather an obligatory step in the maturation of the protein, that could also be necessary for other genes' expressions.)
To be a bit more precise, I am thinking about a metabolic system where the expressions of most of the involved genes are regulated by a master transcriptional regulator (SurR, an ArsR-type, redox-active regulator involved in Thermococcales’ (Archaea) energy metabolism).
I am wondering what kind of effects a change in the expression of the regulator-encoding gene could have on the whole system. And before getting to an effect on the regulon, I guess it is a good idea to start with the regulator itself: could it be theoretically fully functional in a greater concentration, if I would only consider overexpressing its gene for example?
One type of heavy post-translational modification is maturation by endopeptidase, which can hamper the correct activity of an enzyme if not considered adequately in a case of, let’s say, overexpression attempt. (this example is particularly important here since several enzymes of the regulon need to be importantly modified post-translationnaly)
Since there does not seem to be enough literature on the particular regulator I am interested about, and since a quick research for answers in other systems was not successful on my side, I am thus asking the SE community if anyone may have known about some kind of maturation-like, post-translational process, which could be needed for a fully functional transcriptional regulator. Would I need to worry about other genes than only the one coding for the regulator, to that extent?