Open AccessPhosphorylation of Escherichia coli poly(A) polymerase I and effects of this modification on the enzyme activity
Author(s) -
Jasiecki Jacek,
Węgrzyn Grzegorz
Publication year - 2006
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2006.00340.x
Subject(s) - phosphorylation , escherichia coli , enzyme , dephosphorylation , rna polymerase , polymerase , biochemistry , in vivo , polyadenylation , chemistry , biology , microbiology and biotechnology , rna , phosphatase , gene , genetics
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.