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  Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins

von Moeller, H., Lerner, R., Ricciardi, A., Basquin, C., Marzluff, W. F., & Conti, E. (2013). Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins. NUCLEIC ACIDS RESEARCH, 41(16), 7960-7971. doi:10.1093/nar/gkt558.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-78D0-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-78D1-0
Genre: Journal Article

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Nucl. Acids Res.-2013-von Moeller-7960-71.pdf (Any fulltext), 13MB
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 Creators:
von Moeller, Holger1, Author              
Lerner, Rachel2, Author
Ricciardi, Adele2, Author
Basquin, Claire1, Author              
Marzluff, William F.2, Author
Conti, Elena1, Author              
Affiliations:
1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
2external, ou_persistent22              

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Free keywords: LOOP BINDING-PROTEIN; HISTONE MESSENGER-RNA; STEM-LOOP; EUKARYOTIC TRANSLATION; CELL-CYCLE; POLY(A)-BINDING PROTEIN; NUCLEOPORIN NUP214; S-PHASE; COMPLEX; INITIATION
 Abstract: In metazoans, replication-dependent histone mRNAs end in a stem-loop structure instead of the poly(A) tail characteristic of all other mature mRNAs. This specialized 3' end is bound by stem-loop binding protein (SLBP), a protein that participates in the nuclear export and translation of histone mRNAs. The translational activity of SLBP is mediated by interaction with SLIP1, a middle domain of initiation factor 4G (MIF4G)-like protein that connects to translation initiation. We determined the 2.5 angstrom resolution crystal structure of zebrafish SLIP1 bound to the translation-activation domain of SLBP and identified the determinants of the recognition. We discovered a SLIP1-binding motif (SBM) in two additional proteins: the translation initiation factor eIF3g and the mRNA-export factor DBP5. We confirmed the binding of SLIP1 to DBP5 and eIF3g by pull-down assays and determined the 3.25 angstrom resolution structure of SLIP1 bound to the DBP5 SBM. The SBM-binding and homodimerization residues of SLIP1 are conserved in the MIF4G domain of CBP80/20-dependent translation initiation factor (CTIF). The results suggest how the SLIP1 homodimer or a SLIP1-CTIF heterodimer can function as platforms to bridge SLBP with SBM-containing proteins involved in different steps of mRNA metabolism.

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Language(s): eng - English
 Dates: 2013-09
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000325173300039
DOI: 10.1093/nar/gkt558
 Degree: -

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Title: NUCLEIC ACIDS RESEARCH
Source Genre: Journal
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Publ. Info: GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND : OXFORD UNIV PRESS
Pages: - Volume / Issue: 41 (16) Sequence Number: - Start / End Page: 7960 - 7971 Identifier: ISSN: 0305-1048