Molecular basis of the divalent cation selectivity of the uridylyltransferase GlnD towards the signal transduction proteins GlnJ and GlnB.
(English)Manuscript (preprint) (Other academic)
PII proteins have a fundamental role in the control of nitrogen metabolism in bacteria, with the PII-target interaction being controlled by metabolite binding and post-translational modification. In the photosynthetic bacterium Rhodospirillum rubrum, the PII proteins GlnB and GlnJ were shown, in spite of their high degree of similarity, to have different requirements for post-translational uridylylation, with respect to the divalent cations, Mg2+ and Mn2+. Given the importance of uridylylation in the functional interactions of PII proteins, we have addressed the molecular basis for that difference and identified two amino acid residues that influence the divalent cation selectivity.
Research subject Biochemistry
IdentifiersURN: urn:nbn:se:su:diva-30810OAI: oai:DiVA.org:su-30810DiVA: diva2:274152