Phosphorylation of Escherichia coli poly(A) polymerase I and effects of this modification on the enzyme activity.
In Escherichia coli, RNA polyadenylation is catalyzed mainly by poly(A) polymerase I (PAP I). Here we demonstrate that a PAP I variant with a C-terminal His tag (PAP I-His) can be phosphorylated both in vivo and in an artificial in vitro system. The in vivo phosphorylation of PAP I-His impairs activity of this enzyme. Previous studies, performed by others, indicated that phosphorylation of His-tagged proteins usually reflects such a modification of their native counterparts in bacterial cells. Therefore, our results suggest that phosphorylation and dephosphorylation of PAP I may be important regulatory processes in the control of activity of this enzyme.
Jasiecki
Jacek
J
Department of Molecular Biology, University of Gdańsk, Gdańsk, Poland.
Wegrzyn
Grzegorz
G
D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D010766:Phosphorylation; D026723:Polyadenylation / Q000502:physiology; D011062:Polynucleotide Adenylyltransferase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D012329:RNA, Bacterial / Q000378:metabolism
D029968:Escherichia coli Proteins; C042027:RNA I; D012329:RNA, Bacterial; D011062:Polynucleotide Adenylyltransferase; C063643:pcnB protein, E coli