Open AccessExpression, crystallization and preliminary crystallographic analysis of RNA‐binding protein Hfq (YmaH) from Bacillus subtilis in complex with an RNA aptamer
Author(s) -
Baba Seiki,
Someya Tatsuhiko,
Kawai Gota,
Nakamura Kouji,
Kumasaka Takashi
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110009942
Subject(s) - rna , bacillus subtilis , microbiology and biotechnology , messenger rna , escherichia coli , rna binding protein , transfer rna , chemistry , biology , crystallography , gene , biochemistry , bacteria , genetics
The Hfq protein is a hexameric RNA‐binding protein which regulates gene expression by binding to RNA under the influence of diverse environmental stresses. Its ring structure binds various types of RNA, including mRNA and sRNA. RNA‐bound structures of Hfq from Escherichia coli and Staphylococcus aureus have been revealed to have poly(A) RNA at the distal site and U‐rich RNA at the proximal site, respectively. Here, crystals of a complex of the Bacillus subtilis Hfq protein with an A/G‐repeat 7‐mer RNA (Hfq–RNA) that were prepared using the hanging‐drop vapour‐diffusion technique are reported. The type 1 Hfq–RNA crystals belonged to space group I 422, with unit‐cell parameters a = b = 123.70, c = 119.13 Å, while the type 2 Hfq–RNA crystals belonged to space group F 222, with unit‐cell parameters a = 91.92, b = 92.50, c = 114.92 Å. Diffraction data were collected to a resolution of 2.20 Å from both crystal forms. The hexameric structure of the Hfq protein was clearly shown by self‐rotation analysis.