Hfq stimulates the activity of the CCA-adding enzyme

BMC Molecular Biology
Marion ScheibeMario Mörl

Abstract

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. Based on the close evolutionary relation of these two nucleotidyltransferases, it was tested whether Hfq is a specific modulator acting exclusively on PAP or whether it also influences the activity of the CCA-adding enzyme. The obtained data indicate that the reaction catalyzed by this enzyme is substantially accelerated in the presence of Hfq. Furthermore, Hfq binds specifically to tRNA transcripts, which seems to be the prerequisite for the observed effect on CCA-addition. The increase of the CCA-addition in the presence of Hfq suggests that this protein acts as a stimulating...Continue Reading

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Feb 20, 2010·BMC Molecular Biology·Jacques Le DeroutEliane Hajnsdorf
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Methods Mentioned

BETA
aminoacylation
electrophoresis

Related Concepts

CCA-adding enzyme, human
PcnB protein, E coli
Hfq protein, E coli
Enzyme Activation
Polynucleotide Adenylyltransferase
Plasma Protein Binding Capacity
RNA Nucleotidyltransferases
Transfer RNA
Substrate Specificity
Escherichia coli Proteins

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