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          Institute: MPI für Entwicklungsbiologie     Collection: Abteilungsunabhängige Arbeitsgruppen     Display Documents

ID: 16396.0, MPI für Entwicklungsbiologie / Abteilungsunabhängige Arbeitsgruppen
Isolation and characterization of Staufen-containing ribonucleoprotein particles from rat brain
Authors:Mallardo, M.; Deitinghoff, A.; Muller, J.; Goetze, B.; Macchi, P.; Peters, C.; Kiebler, M. A.
Date of Publication (YYYY-MM-DD):2003-02-18
Title of Journal:Proceedings of the National Academy of Sciences of the United States of America
Journal Abbrev.:Proc. Natl. Acad. Sci. U. S. A.
Issue / Number:4
Start Page:2100
End Page:2105
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Localized mRNAs are thought to be transported in defined particles to their final destination. These particles represent large protein complexes that may be involved in recognizing, transporting, and anchoring localized messages. Few components of these ribo-nucleoparticles, however, have been identified yet. We chose the strategy to biochemically enrich native RNA- protein complexes involved in RNA transport to identify the associated RNAs and proteins. Because Staufen proteins were implicated in intracellular RNA transport, we chose mammalian Staufen proteins as markers for the purification of RNA transport particles. Here, we present evidence that Staufen proteins exist in two different complexes: (i) distinct large, ribosome- and endoplasmic reticulum-containing granules preferentially found in the membrane pellets during differential centrifugation and (it) smaller particles in the S100 from rat brain homogenates. On gel filtration of the S100, we identified soluble 670-kDa Staufen1-containing and 440-kDa Staufen2-containing particles. They do not cofractionate with ribosomes and endoplasmic reticulum but rather coenrich with kinesin heavy chain. Furthermore, the fractions containing the Staufen1 particles show a 15-fold enrichment of mRNAs compared with control fractions. Most importantly, these fractions are highly enriched in BC1, and, to a lesser extent, in the alpha- subunit of the Ca2+/calmodulin-dependent kinase II, two dendritically localized RNAs. Finally, both RNAs colocalize with Staufen1-hemagglutinin in particles in dendrites of transfected hippocampal neurons. We therefore propose that these Staufen1-containing particles may represent RNA transport intermediates that are in transit to their final destination within neurons.
Free Keywords:Ca2+/calmcdulin-dependent kinase 11; double-stranded RNA- binding protein; dendritic mRNA transport; BC1
Comment of the Author/Creator:Date: 2003, FEB 18
External Publication Status:published
Document Type:Article
Affiliations:MPI für Entwicklungsbiologie/Abteilungsunabhängige Arbeitsgruppen
External Affiliations:Max Planck Inst Dev Biol, D-72076 Tubingen, Germany; Max Planck Inst Dev Biol, D-72076 Tubingen, Germany; Max Planck Gesell, Friedrich Miescher Lab, D-72076 Tubingen, Germany
Identifiers:ISI:000181073000117 [ID No:1]
ISSN:0027-8424 [ID No:2]
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