Thursday, May 4, 2017

Nature Structural & Molecular Biology Contents: 2017 Volume #24 pp 431 - 490

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Nature Structural & Molecular Biology

Nature Milestones: Antibodies 

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May 2017 Volume 24, Issue 5

News and Views
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Anna Tramontano 1957-2017   pp431 - 432
Janet M Thornton, Alfonso Valencia and Torsten Schwede

News and Views


Carb cutting works better with a partner   pp433 - 435
Jennifer J Kohler
O-GlcNAc is a reversible post-translational modification that is added by O-GlcNAc transferase (OGT) and removed by O-GlcNAcase (OGA). OGA is emerging as a therapeutic target for multiple diseases, but its structure has been elusive until now.

Splicing of Ezh1 gets muscle out of stressful situations   pp435 - 437
Marjorie Brand and F Jeffrey Dilworth
As cells undergo terminal differentiation, the composition of Polycomb-repressive complex 2 (PRC2) changes and the histone H3K27 methyltransferase Ezh2 is progressively replaced by its homolog Ezh1. By identifying an enzymatically inactive splice variant of Ezh1 that is sensitive to cellular stress, Bodega et al. now demonstrate that PRC2-Ezh1 has an essential role in establishing an altered gene expression program required for postmitotic muscle cells to adapt to environmental changes.

See also: Article by Bodega et al.

Capturing heterogeneity: single-cell structures of the 3D genome   pp437 - 438
Elzo de Wit
One of the striking features of cells seen through a microscope is the heterogeneous organization of the nuclei. A combination of molecular methods and computational modeling has now been used to reconstruct accurate 3D structures of the genome inside single nuclei.


DNA-RNA hybrids: the risks of DNA breakage during transcription   pp439 - 443
Andrés Aguilera and Belen Gómez-González
In this Perspective, the authors consider how DNA breaks stimulate R-loop formation, particularly within actively transcribed genomic regions, and discuss the cellular mechanisms that prevent or remove RNA-DNA hybrids to preserve genome integrity.

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A cytosolic Ezh1 isoform modulates a PRC2-Ezh1 epigenetic adaptive response in postmitotic cells   pp444 - 452
Beatrice Bodega, Federica Marasca, Valeria Ranzani, Alessandro Cherubini, Francesco Della Valle et al.
A cytosolic isoform of Ezh1 that lacks the catalytic domain controls nuclear PRC2 activity in response to atrophic oxidative stress in skeletal muscle cells by trapping Eed in the cytoplasm.

See also: News and Views by Brand & Dilworth

Structure of the 40S-ABCE1 post-splitting complex in ribosome recycling and translation initiation   pp453 - 460
Andre Heuer, Milan Gerovac, Christian Schmidt, Simon Trowitzsch, Anne Preis et al.
Cryo-EM structures of the yeast 40S in complex with ribosome-splitting protein ABCE1, along with functional analyses, reveal that the FeS cluster domain undergoes a 150° rotation to dissociate ribosomal subunits.

Intraflagellar transport dynein is autoinhibited by trapping of its mechanical and track-binding elements   pp461 - 468
Katerina Toropova, Miroslav Mladenov and Anthony J Roberts
Molecular motor dynein-2, involved in retrograde intraflagellar transport, adopts an autoinhibited conformation, in which the mechanical linker and track-binding stalk are trapped via a newly described motor-motor interface.

Structural basis for lipopolysaccharide extraction by ABC transporter LptB2FG   pp469 - 474
Qingshan Luo, Xu Yang, Shan Yu, Huigang Shi, Kun Wang et al.
The crystal structure of LptB2FG, an ABC transporter that extracts LPS from the bacterial inner membrane and transports it to the outer membrane, indicates a transport mechanism distinct from classical ABC transporters.

Parkin-phosphoubiquitin complex reveals cryptic ubiquitin-binding site required for RBR ligase activity   pp475 - 483
Atul Kumar, Viduth K Chaugule, Tara E C Condos, Kathryn R Barber, Clare Johnson et al.
The human RBR E3 ligase Parkin is captured in complex with phosphoubiquitin, revealing a cryptic ubiquitin-binding site and indicating a mechanism of cooperation between RBR modules for activation.

An orthogonal single-molecule experiment reveals multiple-attempt dynamics of type IA topoisomerases   pp484 - 490
Kathryn H Gunn, John F Marko and Alfonso Mondragon
A novel combination of magnetic tweezers and single-molecule TIRF microscopy reveals that topoisomerase IA makes multiple attempts to engage DNA before successfully catalyzing strand passage and DNA relaxation.

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