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Heym, R.G. ; Zimmermann, D.* ; Edelmann, F. ; Israel, L.* ; Ökten, Z.* ; Kovar, D.R.* ; Niessing, D.

In vitro reconstitution of an mRNA-transport complex reveals mechanisms of assembly and motor activation.

J. Cell Biol. 203, 971-984 (2013)
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The assembly and composition of ribonucleic acid (RNA)-transporting particles for asymmetric messenger RNA (mRNA) localization is not well understood. During mitosis of budding yeast, the Swi5p-dependent HO expression (SHE) complex transports a set of mRNAs into the daughter cell. We recombinantly reconstituted the core SHE complex and assessed its properties. The cytoplasmic precomplex contains only one motor and is unable to support continuous transport. However, a defined interaction with a second, RNA-bound precomplex after its nuclear export dimerizes the motor and activates processive RNA transport. The run length observed in vitro is compatible with long-distance transport in vivo. Surprisingly, SHE complexes that either contain or lack RNA cargo show similar motility properties, demonstrating that the RNA-binding protein and not its cargo activates motility. We further show that SHE complexes have a defined size but multimerize into variable particles upon binding of RNAs with multiple localization elements. Based on these findings, we provide an estimate of number, size, and composition of such multimeric SHE particles in the cell.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Class-v Myosin; Budding Yeast; Binding Protein; Saccharomyces-cerevisiae; Ribonucleoprotein Complexes; Dependent Localization; Structural Elements; Monomeric Myosin; Recombinant Rna; Globular Tail
ISSN (print) / ISBN 0021-9525
e-ISSN 1540-8140
Quellenangaben Band: 203, Heft: 6, Seiten: 971-984 Artikelnummer: , Supplement: ,
Verlag Rockefeller University Press
Begutachtungsstatus Peer reviewed