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Volume 11 Issue 3, March 2004

Two independent studies report the identification of a new component in the mitochondrial import machinery of the inner membrane. This protein is a cochaperone and is essential for transporting polypeptides into the matrix. A model with all known components in this machinery is shown (lower right; the proteins facing the intermembrane space are yellow and the translocating preprotein is red), together with an image of the mitochondrion reconstructed from electron tomography (courtesy of G.A. Perkins & T.G. Frey). See pp 226-233 and 234-241.

Volume 11 Issue 3

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Editorial

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Meeting Report

  • Gene expression is a highly interconnected multistep process. A recent meeting in Iguazu Falls, Argentina, highlighted the need to uncover both the molecular details of each single step as well as the mechanisms of coordination among processes in order to fully understand the expression of genes.

    • Tom Misteli
    Meeting Report
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News & Views

  • The ribosome must be very selective for aminoacyl-tRNAs while maintaining a rapid rate of protein synthesis. A recent kinetic study reveals how it is able to make quick and accurate decisions to maintain high fidelity.

    • Luke D Sherlin
    • Olke C Uhlenbeck
    News & Views

  • One of many consequences of heat shock is a general and profound inhibition of pre-mRNA splicing. In mammalian cells, this inhibition is mediated by a specific member of the SR protein family of splicing factors, which becomes a splicing repressor upon heat-triggered dephosphorylation.

    • Timothy W Nilsen
    News & Views

  • A recent study on the RNA-binding protein Npl3p reveals how its direct interaction with the mRNA export receptor Mex67p is regulated by phosphorylation and how this post-translational modification contributes to the assembly and disassembly of mRNP export complexes.

    • Elisa Izaurralde
    News & Views
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