Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review
Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA. / Andersen, Christian Brix Folsted; Ballut, Lionel; Johansen, Jesper Sanderhoff et al.
I: Science, Bind 313, 2006, s. 1968-1972.Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review
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TY - JOUR
T1 - Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA
AU - Andersen, Christian Brix Folsted
AU - Ballut, Lionel
AU - Johansen, Jesper Sanderhoff
AU - Chamieh, H.
AU - Nielsen, Klaus Hvid
AU - Oliveira, Cristiano
AU - Pedersen, Jan Skov
AU - Seraphin, B.
AU - LeHir, H.
AU - Andersen, Gregers Rom
PY - 2006
Y1 - 2006
N2 - In higher eukaryotes, a multiprotein exon junction complex is deposited on spliced messenger RNAs. The complex is organized around a stable core, which serves as a binding platform for numerous factors that influence messenger RNA function. Here, we present the crystal structure of a tetrameric exon junction core complex containing the DEAD-box adenosine triphosphatase (ATPase) eukaryotic initiation factor 4AIII (eIF4AIII) bound to an ATP analog, MAGOH, Y14, a fragment of MLN51, and a polyuracil mRNA mimic. eIF4AIII interacts with the phosphate-ribose backbone of six consecutive nucleotides and prevents part of the bound RNA from being double stranded. The MAGOH and Y14 subunits lock eIF4AIII in a prehydrolysis state, and activation of the ATPase probably requires only modest conformational changes in eIF4AIII motif I.
AB - In higher eukaryotes, a multiprotein exon junction complex is deposited on spliced messenger RNAs. The complex is organized around a stable core, which serves as a binding platform for numerous factors that influence messenger RNA function. Here, we present the crystal structure of a tetrameric exon junction core complex containing the DEAD-box adenosine triphosphatase (ATPase) eukaryotic initiation factor 4AIII (eIF4AIII) bound to an ATP analog, MAGOH, Y14, a fragment of MLN51, and a polyuracil mRNA mimic. eIF4AIII interacts with the phosphate-ribose backbone of six consecutive nucleotides and prevents part of the bound RNA from being double stranded. The MAGOH and Y14 subunits lock eIF4AIII in a prehydrolysis state, and activation of the ATPase probably requires only modest conformational changes in eIF4AIII motif I.
KW - splicing
KW - mRNA metabolism
KW - DEAD-box
M3 - Journal article
VL - 313
SP - 1968
EP - 1972
JO - Science
JF - Science
SN - 0036-8075
ER -