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Volume 23 Issue 3, March 2016

Cryo-EM structure of the yeast CMG reveals two Mcm2-7 helicase conformations and an Mcm5-subunit domain inserted into the central channel, thus shedding light onto how CMG unwinds dsDNA. Cover image by © urfingus / iStock / Thinkstock. (p 217)

News & Views

  • 50 years ago, Jardetzky proposed the alternating-access model, which has shaped the theoretical understanding of how substrates are carried across cell membranes. Two studies now demonstrate that transporters from distinct families undergo unexpectedly large elevator-like movements and also suggest that an 'elevate and twist' mechanism is a common means of achieving alternating access across the membrane.

    • Renae M Ryan
    • Robert J Vandenberg
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  • During assembly of spliceosomal small nuclear ribonucleoproteins (snRNPs), the RNA-binding protein (RBP) Gemin5 recognizes the snRNP code and interacts with the large Gemin2–SMN complex. So et al. now find that Gemin2 also interacts with U1-70K, thereby conferring a preferential advantage on U1 snRNP assembly, and they extrapolate that SMN–Gemin2 serves a general ribonucleoprotein-exchange function.

    • Megan Mayerle
    • Christine Guthrie
    News & Views
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