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<article-id pub-id-type="publisher-id">040549897</article-id>
<copyright-statement>Copyright &#x00A9; 2000, The 
National Academy of Sciences</copyright-statement>
<p>Current evidence suggests that the length of poly(A) tails 
of bacterial mRNAs result from a competition between poly(A) polymerase 
and exoribonucleases that attack the 3&#x2032; ends of RNAs. Here, we 
show that host factor Hfq is also involved in poly(A) tail metabolism. 
Inactivation of the <italic>hfq</italic> gene reduces the length of 
poly(A) tails synthesized at the 3&#x2032; end of the <italic>rpsO</italic> 
mRNA by poly(A) polymerase I <italic>in vivo</italic>. <italic>In vitro</italic>,
Hfq stimulates synthesis of long tails by poly(A) polymerase I. The strong
binding of Hfq to oligoadenylated RNA probably explains why it stimulates
elongation of primers that already harbor tails of 20&#x2013;35 A.
Polyadenylation becomes processive in the presence of Hfq. The similar
properties of Hfq and the PABPII poly(A) binding protein, which stimulates
poly(A) tail elongation in mammals, indicates that similar mechanisms control
poly(A) tail synthesis in prokaryotes and eukaryotes.</p>