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Volume 15 Issue 3, March 2008

The eukaryotic proteasome catalyzes the selective degradation of targeted proteins. New structural and functional work reveals the role of a chaperone complex in directing assembly of the proteasome core, or 20S, particle. Cover by Erin Boyle shows the 20S proteasome with the chaperone complex, in the style of artist Mark Rothko. pp 228 and 237, News and Views p 218

Volume 15 Issue 3

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Editorial

  • The current move toward a presidential debate highlighting science and technology may at least provide the impetus for political discussion in these areas to go beyond hot button issues.

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News & Views

  • Assembly of the 34-subunit, 2.5 megadalton 26S proteasome starts with formation of the seven-membered α-ring. A set of newly identified proteasome chaperones serves as a clamp to seal α-rings with the correct composition. By regulating the efficiency and outcome of this crucial step in proteasome biogenesis, these dedicated proteasome chaperones apparently partake in the stress response and in adaptation to intracellular proteolysis needs.

    • Rina Rosenzweig
    • Michael H Glickman
    News & Views

  • The ankyrin repeats of the G9a and GLP histone methyltransferases have now been shown to be binding modules for mono- and dimethyllysine histone H3 lysine 9 (H3K9), revealing a new function for an ankyrin repeat domain and showing that a polypeptide chain can both create and recognize the same histone mark.

    • Michael M Brent
    • Ronen Marmorstein
    News & Views

  • The compositional complexity of the spliceosome creates a serious obstacle for its experimental analysis. Purification of a compositionally defined splicing complex C capable of completing the second step of splicing in the absence of additional proteins opens the door for future mechanistic and structural analyses.

    • Maria M Konarska
    News & Views

  • The kinase regulatory-loop binding (KRLB) region of insulin receptor substrate 2 was originally thought to be a new type of domain with binding properties similar to phosphotyrosine binding (PTB) domains. A crystallographic study now shows that KRLB is actually a short peptide segment that binds to the insulin receptor using an extended series of contacts that mimic both autoinhibitory loop and ATP binding to its catalytic cleft.

    • Sang Youn Park
    • Steven E Shoelson
    News & Views
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