Journal
NUCLEIC ACIDS RESEARCH
Volume 40, Issue 21, Pages 11023-11035Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gks809
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Funding
- American Heart Association [09 GRNT2280109]
- National Institutes of Health [AI-064564]
- Danish Natural Science Research Council
- Robert A. Welch Foundation [G-0040]
- Office of science, Office of Basic Energy Sciences, Material Sciences Division, of the US Department of Energy, Lawrence Berkeley National Laboratory [DE-AC03-76SF00098]
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Hfq is a post-transcriptional regulator that plays a key role in bacterial gene expression by binding AU-rich sequences and A-tracts to facilitate the annealing of sRNAs to target mRNAs and to affect RNA stability. To understand how Hfq from the Gram-positive bacterium Staphylococcus aureus (Sa) binds A-tract RNA, we determined the crystal structure of an Sa Hfq-adenine oligoribonucleotide complex. The structure reveals a bipartite RNA-binding motif on the distal face that is composed of a purine nucleotide-specificity site (R-site) and a non-discriminating linker site (L-site). The (R-L)-binding motif, which is also utilized by Bacillus subtilis Hfq to bind (AG)(3)A, differs from the (A-R-N) tripartite poly(A) RNA-binding motif of Escherichia coli Hfq whereby the Sa Hfq R-site strongly prefers adenosine, is more aromatic and permits deeper insertion of the adenine ring. R-site adenine-stacking residue Phe30, which is conserved among Gram-positive bacterial Hfqs, and an altered conformation about beta 3 and beta 4 eliminate the adenosine-specificity site (A-site) and create the L-site. Binding studies show that Sa Hfq binds (AU)(3)A approximate to (AG)(3)A >= (AC)(3)A > (AA)(3)A and L-site residue Lys33 plays a significant role. The (R-L) motif is likely utilized by Hfqs from most Gram-positive bacteria to bind alternating (A-N)(n) RNA.
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