Uridylylation of the PII protein from Herbaspirillum seropedicae.
The PII protein is apparently involved in the control of NifA activity in Herbaspirillum seropedicae. To evaluate the probable role of PII in signal transduction, uridylylation assays were conducted with purified H. seropedicae PII and Escherichia coli GlnD, or a cell-free extract of H. seropedicae as sources of uridylylating activity. The results showed that alpha-ketoglutarate and ATP stimulate uridylylation whereas glutamine inhibits uridylylation. Deuridylylation of PII-UMP was dependent on glutamine and inhibited by ATP and alpha-ketoglutarate. PII uridylylation and (or) deuridylylation in response to these effectors suggests that PII is a nitrogen level signal transducer in H. seropedicae.
Benelli
E M
EM
Department of Biochemistry, Federal University of Parana, Curitiba, Brazil.
Buck
M
M
de Souza
E M
EM
Yates
M G
MG
Pedrosa
F O
FO
D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D020562:Betaproteobacteria / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D005973:Glutamine / Q000378:metabolism; D007656:Ketoglutaric Acids / Q000378:metabolism; D009713:Nucleotidyltransferases / Q000378:metabolism; D051922:PII Nitrogen Regulatory Proteins; D015398:Signal Transduction; D014542:Uridine Monophosphate / Q000378:metabolism*
D001426:Bacterial Proteins; D007656:Ketoglutaric Acids; D051922:PII Nitrogen Regulatory Proteins; D005973:Glutamine; C404143:PIID regulatory protein, Bacteria; D000255:Adenosine Triphosphate; D014542:Uridine Monophosphate; D009713:Nucleotidyltransferases; C022515:regulatory protein uridylyltransferase