Structure of an Escherichia coli Hfq:RNA complex at 0.97 Å resolution

TY - JOUR

T1 - Structure of an Escherichia coli Hfq:RNA complex at 0.97 Å resolution

AU - Schulz, Eike C

AU - Barabas, Orsolya

PY - 2014/11

Y1 - 2014/11

N2 - In bacteria, small RNAs (sRNAs) silence or activate target genes through base pairing with the mRNA, thereby modulating its translation. A central player in this process is the RNA chaperone Hfq, which facilitates the annealing of sRNAs with their target mRNAs. Hfq has two RNA-binding surfaces that recognize A-rich and U-rich sequences, and is believed to bind an sRNA-mRNA pair simultaneously. However, how Hfq promotes annealing remains unclear. Here, the crystal structure of Escherichia coli Hfq is presented in complex with U6-RNA bound to its proximal binding site at 0.97 Å resolution, revealing the Hfq-RNA interaction in exceptional detail.

AB - In bacteria, small RNAs (sRNAs) silence or activate target genes through base pairing with the mRNA, thereby modulating its translation. A central player in this process is the RNA chaperone Hfq, which facilitates the annealing of sRNAs with their target mRNAs. Hfq has two RNA-binding surfaces that recognize A-rich and U-rich sequences, and is believed to bind an sRNA-mRNA pair simultaneously. However, how Hfq promotes annealing remains unclear. Here, the crystal structure of Escherichia coli Hfq is presented in complex with U6-RNA bound to its proximal binding site at 0.97 Å resolution, revealing the Hfq-RNA interaction in exceptional detail.

KW - Crystallography, X-Ray

KW - Escherichia coli/genetics

KW - Escherichia coli Proteins/chemistry

KW - Host Factor 1 Protein/chemistry

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

KW - RNA, Bacterial/chemistry

U2 - 10.1107/S2053230X14020044

DO - 10.1107/S2053230X14020044

M3 - SCORING: Journal article

C2 - 25372815

VL - 70

SP - 1492

EP - 1497

JO - ACTA CRYSTALLOGR F

JF - ACTA CRYSTALLOGR F

SN - 2053-230X

IS - Pt 11

ER -