Publikationsdatum:
2006-08-26
Beschreibung:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Andersen, Christian B F -- Ballut, Lionel -- Johansen, Jesper S -- Chamieh, Hala -- Nielsen, Klaus H -- Oliveira, Cristiano L P -- Pedersen, Jan Skov -- Seraphin, Bertrand -- Le Hir, Herve -- Andersen, Gregers Rom -- New York, N.Y. -- Science. 2006 Sep 29;313(5795):1968-72. Epub 2006 Aug 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Aarhus, DK-8000 Aarhus, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16931718" target="_blank"〉PubMed〈/a〉
Schlagwort(e):
Adenosine Triphosphate/analogs & derivatives/metabolism
;
Adenylyl Imidodiphosphate/metabolism
;
Amino Acid Motifs
;
Amino Acid Sequence
;
Animals
;
Crystallography, X-Ray
;
DEAD-box RNA Helicases
;
Dimerization
;
Drosophila Proteins/chemistry/metabolism
;
Eukaryotic Initiation Factor-4A/*chemistry/metabolism
;
*Exons
;
Humans
;
Hydrogen Bonding
;
Hydrolysis
;
Models, Molecular
;
Molecular Sequence Data
;
Mutation
;
Neoplasm Proteins/*chemistry/metabolism
;
Nuclear Proteins/*chemistry/metabolism
;
Nucleic Acid Conformation
;
Poly U/*chemistry/metabolism
;
Protein Conformation
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
RNA Helicases/chemistry/metabolism
;
RNA, Messenger/*chemistry/metabolism
;
RNA-Binding Proteins/*chemistry/metabolism
Print ISSN:
0036-8075
Digitale ISSN:
1095-9203
Thema:
Biologie
,
Chemie und Pharmazie
,
Informatik
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
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