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Volume 21 Issue 8, August 2014

PUF proteins are single-stranded RNA-binding proteins that contain multiple repeat elements, each of which contains a tripartite amino acid motif that dictates the identity of the targeted RNA base. Wickens and colleagues analyze the specificities of two dozen PUF proteins to create a palette of RNA specificities that can be used to design new proteins tailored to RNA targets. Cover image from Kasia75/iStock/Thinkstock. pp 732–738, News and Views p 653

News & Views

  • Two sibling DNA polymerases synthesize most of the eukaryotic nuclear genome. A new study provides insights into the distinct protein interactions that deliver these replicases for asymmetric leading- and lagging-strand replication and reveals possible cross-talk between DNA replication and other cellular processes.

    • Thomas A Kunkel
    • Peter M Burgers
    News & Views

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  • The development of new strategies to deplete maternal histone proteins in vivo and in vitro has led to the discovery of unexpected roles of histones in forming a functional nuclear envelope.

    • Peter J Skene
    • Steven Henikoff
    News & Views
  • Classical PUF proteins bind to single-stranded RNA with sequence specificity that can be engineered by site-directed mutagenesis according to a simple RNA-recognition code. Now in-depth probing of the PUF RNA-recognition code enhances future design of PUF proteins and exposes hidden complexity in generating specificity.

    • Traci M Tanaka Hall
    News & Views
  • Mechanisms of DNA damage repair within actively transcribed genes are poorly understood. Five new reports shed light on the contributions of chromatin to this process by uncovering roles for histone H3 Lys36 methylation, a post-translational modification previously linked to transcription elongation, in the control of DNA-damage signaling and double strand break repair.

    • Deepak K Jha
    • Sophia X Pfister
    • Brian D Strahl
    News & Views
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