Cooperation of Escherichia coli Hfq hexamers in DsrA binding.

Szczegóły
Abstrakt

Tytuł:: Cooperation of Escherichia coli Hfq hexamers in DsrA binding.
Autorzy:: Wang W; Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.
Wang L
Zou Y
Zhang J
Gong Q
Wu J
Shi Y
Źródło:: Genes & development [Genes Dev] 2011 Oct 01; Vol. 25 (19), pp. 2106-17.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Publication: Cold Spring Harbor, NY : Cold Spring Harbor Laboratory Press
Original Publication: [Cold Spring Harbor, N.Y.] : Cold Spring Harbor Laboratory in association with the Genetical Society of Great Britain, [c1987-
MeSH Terms:: Models, Molecular*
Escherichia coli/*metabolism
Escherichia coli Proteins/*chemistry
Host Factor 1 Protein/*chemistry
RNA, Small Untranslated/*metabolism
Adenosine Diphosphate/metabolism ; Binding Sites ; Polymers ; Protein Binding ; Protein Structure, Tertiary
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Substance Nomenclature:: 0 (DsrA RNA, E coli)
0 (Escherichia coli Proteins)
0 (Hfq protein, E coli)
0 (Host Factor 1 Protein)
0 (Polymers)
0 (RNA, Small Untranslated)
61D2G4IYVH (Adenosine Diphosphate)
Entry Date(s):: Date Created: 20111008 Date Completed: 20111128 Latest Revision: 20230810
Update Code:: 20240104
PubMed Central ID:: PMC3197208
DOI:: 10.1101/gad.16746011
PMID:: 21979921
: Czasopismo naukowe

Hfq is a bacterial post-transcriptional regulator. It facilitates base-pairing between sRNA and target mRNA. Hfq mediates DsrA-dependent translational activation of rpoS mRNA at low temperatures. rpoS encodes the stationary-phase σ factor σ(S), which is the central regulator in general stress response. However, structural information on Hfq-DsrA interaction is not yet available. Although Hfq is reported to hydrolyze ATP, the ATP-binding site is still unknown. Here, we report a ternary crystal complex structure of Escherichia coli Hfq bound to a major Hfq recognition region on DsrA (AU(6)A) together with ADP, and a crystal complex structure of Hfq bound to ADP. AU(6)A binds to the proximal and distal sides of two Hfq hexamers. ADP binds to a purine-selective site on the distal side and contacts conserved arginine or glutamine residues on the proximal side of another hexamer. This binding mode is different from previously postulated. The cooperation of two different Hfq hexamers upon nucleic acid binding in solution is verified by fluorescence polarization and solution nuclear magnetic resonance (NMR) experiments using fragments of Hfq and DsrA. Fluorescence resonance energy transfer conducted with full-length Hfq and DsrA also supports cooperation of Hfq hexamers upon DsrA binding. The implications of Hfq hexamer cooperation have been discussed.

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