Hfq stimulates the activity of the CCA-adding enzyme |
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Authors: | Marion Scheibe Sonja Bonin Eliane Hajnsdorf Heike Betat Mario Mörl |
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Affiliation: | 1.Institute for Biochemistry, University of Leipzig,Leipzig,Germany;2.UPR 9073 CNRS conventionnée avec l'Université Paris 7-Denis Diderot, Institut de Biologie Physico-Chimique,Paris,France |
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Abstract: | Background The bacterial Sm-like protein Hfq is known as an important regulator involved in many reactions of RNA metabolism. A prominent function of Hfq is the stimulation of RNA polyadenylation catalyzed by E. coli poly(A) polymerase I (PAP). As a member of the nucleotidyltransferase superfamily, this enzyme shares a high sequence similarity with an other representative of this family, the tRNA nucleotidyltransferase that synthesizes the 3'-terminal sequence C-C-A to all tRNAs (CCA-adding enzyme). Therefore, it was assumed that Hfq might not only influence the poly(A) polymerase in its specific activity, but also other, similar enzymes like the CCA-adding enzyme. |
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