Thursday, August 3, 2017

Nature Structural & Molecular Biology Contents: 2017 Volume #24 pp 607 - 681

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August 2017 Volume 24, Issue 8

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A tetrad of chromatin interactions for chromosome pairing in X inactivation   pp607 - 608
Ivan Krivega and Ann Dean
An unusual pairing of homologous X chromosomes occurs during X inactivation. A new study in mouse embryonic stem cells shows that telomeres and the telomeric RNA PAR-TERRA are responsible for additional pairwise interactions that guide Xic-Xic pairing.

See also: Article by Chu et al.

Dueling RNA-binding proteins promote translational activation   pp609 - 610
Paul Lasko
Meiotic progression is controlled by cytoplasmic polyadenylation and translational activation of masked, maternal mRNAs. RNA-binding-protein interactions with adjacent cis elements cause local conformational changes to the mRNAs that determine the extent and timing of their activation.

See also: Article by Weill et al.


Two chaperones locked in an embrace: structure and function of the ribosome-associated complex RAC   pp611 - 619
Ying Zhang, Irmgard Sinning and Sabine Rospert
The ribosome-associated complex (RAC) is formed by the JD protein Zuo1 and the unconventional Hsp70 Ssz1. This Review presents recent developments that have increased our understanding of RAC's mechanisms and cellular functions.

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PAR-TERRA directs homologous sex chromosome pairing   pp620 - 631
Hsueh-Ping Chu, John E Froberg, Barry Kesner, Hyun Jung Oh, Fei Ji et al.
New analyses reveal that TERRA transcripts arising from the subtelomeric pseudoautosomal (PAR) region of sex chromosomes nucleate pairing of X alleles in mouse ES cells.

See also: News and Views by Krivega & Dean

Asparagine endopeptidase cleaves α-synuclein and mediates pathologic activities in Parkinson's disease   pp632 - 642
Zhentao Zhang, Seong Su Kang, Xia Liu, Eun Hee Ahn, Zhaohui Zhang et al.
Asparagine endopeptidase (AEP) cleaves human α-synuclein at Asn103, yielding a fragment with higher aggregation propensity than that of the full-length protein. Truncated α-synuclein is also more neurotoxic and leads to dopaminergic neuronal loss and motor impairments in mice.

Regulator-dependent mechanisms of C3b processing by factor I allow differentiation of immune responses   pp643 - 651
Xiaoguang Xue, Jin Wu, Daniel Ricklin, Federico Forneris, Patrizia Di Crescenzio et al.
The structure of C3b in complex with factor I and a shortened version of factor H, along with functional analyses, leads to a mechanistic model for how regulators determine sequential cleavage events on C3b.

Mechanochemical evolution of the giant muscle protein titin as inferred from resurrected proteins   pp652 - 657
Aitor Manteca, Jorg Schonfelder, Alvaro Alonso-Caballero, Marie J Fertin, Nerea Barruetabeña et al.
Single-molecule spectroscopy analyses of titin fragments from modern animals and reconstructed from the last common ancestors to mammals, sauropsids and tetrapods shed light on the evolution of the mechanical properties of muscle titin from the Paleozoic to our days.

Multi-domain utilization by TUT4 and TUT7 in control of let-7 biogenesis   pp658 - 665
Christopher R Faehnle, Jack Walleshauser and Leemor Joshua-Tor
Structural analysis of the uridyl transferases TUT4 and TUT7 reveals the use of two functional modules in the switch from monouridylation of pre-let-7, which promotes let-7 expression, to oligouridylation of pre-let-7, which marks it for degradation.

A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer   pp666 - 671
Rosanna M Robertson, Jiangwei Yao, Stefan Gajewski, Gyanendra Kumar, Erik W Martin et al.
The crystal structure of Thermotoga maritima lysophosphatidic acid acyltransferase reveals a two-helix motif that positions the active site for catalysis within the membrane bilayer.

Musashi 1 regulates the timing and extent of meiotic mRNA translational activation by promoting the use of specific CPEs   pp672 - 681
Laure Weill, Eulàlia Belloc, Chiara Lara Castellazzi and Raúl Méndez
New data reveal how Musashi binding to Xenopus oocyte mRNAs promotes changes in RNA secondary structure that modulate CPEB1 binding and influence polyadenylation and translational efficiency.

See also: News and Views by Lasko

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