9GU5

Crystal Structure of Hfq V22A

9GU5 の概要

• エントリーDOI: 10.2210/pdb9gu5/pdb
• 分子名称: RNA-binding protein Hfq, RNA (5'-R(P*AP*AP*AP*A)-3'), MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: rna-chaperone, hydrolase
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 135111.78

構造登録者

McQuail, J.,Krepl, M.,Katsuya-Gaviria, K.,Tabib-Salazar, A.,Burchell, L.,Bischler, T.,Grafenhan, T.,Brear, P.,Luisi, B. (登録日: 2024-09-18, 公開日: 2025-02-05)

主引用文献

McQuail, J.,Krepl, M.,Katsuya-Gaviria, K.,Tabib-Salazar, A.,Burchell, L.,Bischler, T.,Grafenhan, T.,Brear, P.,Sponer, J.,Luisi, B.F.,Wigneshweraraj, S.
Transcriptome-scale analysis uncovers conserved residues in the hydrophobic core of the bacterial RNA chaperone Hfq required for small regulatory RNA stability.
Nucleic Acids Res., 53:-, 2025

PubMed Abstract: The RNA chaperone Hfq plays crucial roles in bacterial gene expression and is a major facilitator of small regulatory RNA (sRNA) action. The toroidal architecture of the Hfq hexamer presents three well-characterized surfaces that allow it to bind sRNAs to stabilize them and engage target transcripts. Hfq-interacting sRNAs are categorized into two classes based on the surfaces they use to bind Hfq. By characterizing a systematic alanine mutant library of Hfq to identify amino acid residues that impact survival of Escherichia coli experiencing nitrogen (N) starvation, we corroborated the important role of the three RNA-binding surfaces for Hfq function. We uncovered two, previously uncharacterized, conserved residues, V22 and G34, in the hydrophobic core of Hfq, to have a profound impact on Hfq's RNA-binding activity in vivo. Transcriptome-scale analysis revealed that V22A and G34A Hfq mutants cause widespread destabilization of both sRNA classes, to the same extent as seen in bacteria devoid of Hfq. However, the alanine substitutions at these residues resulted in only modest alteration in stability and structure of Hfq. We propose that V22 and G34 have impact on Hfq function, especially critical under cellular conditions when there is an increased demand for Hfq, such as N starvation.

PubMed: 39868539
DOI: 10.1093/nar/gkaf019

実験手法

X-RAY DIFFRACTION (2.9 Å)