Wednesday, March 2, 2016

Nature Structural & Molecular Biology Contents: 2016 Volume #23 pp 187-263

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This special Focus highlights the unprecedented insights gained into the regulatory mechanisms underlying nuclear reprogramming, pluripotency and cell identity, and looks at the progress and challenges in using embryonic stem (ES) cells and iPSCs for therapeutic applications. Available free online

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TABLE OF CONTENTS

March 2016 Volume 23, Issue 3

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The term genetic engineering has been around since the 1970s, but it is only in the past few years that researchers have developed the tools to allow them to engineer the genome with the precision that they had originally envisaged.  This Nature Outlook looks at the risks and benefits of genome editing. Available free online.

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Elevating the alternating-access model   pp187 - 189
Renae M Ryan and Robert J Vandenberg
doi:10.1038/nsmb.3179
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.

See also: Article by Coincon et al. | Article by Mulligan et al.

A new communication hub in the RNA world   pp189 - 190
Megan Mayerle and Christine Guthrie
doi:10.1038/nsmb.3178
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.

See also: Article by So et al.

Using T cells to detect noncanonical translation   p191
Katrina Woolcock
doi:10.1038/nsmb0316-191

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Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins   pp192 - 196
Long Han, Jiangge Zheng, Yan Wang, Xu Yang, Yanqing Liu, Chuanqi Sun, Baohua Cao, Haizhen Zhou, Dongchun Ni, Jizhong Lou, Yongfang Zhao & Yihua Huang
doi:10.1038/nsmb.3181
The crystal structure of the full five-subunit BAM complex from Escherichia coli reveals the interactions between individual components and domains and provides insights into the biogenesis of β-barrel outer-membrane proteins.

Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor   pp197 - 203
Matthew A B Baker, Robert M G Hynson, Lorraine A Ganuelas, Nasim Shah Mohammadi, Chu Wai Liew, Anthony A Rey, Anthony P Duff, Andrew E Whitten, Cy M Jeffries, Nicolas J Delalez, Yusuke V Morimoto, Daniela Stock, Judith P Armitage, Andrew J Turberfield, Keiichi Namba, Richard M Berry & Lawrence K Lee
doi:10.1038/nsmb.3172
A combination of evolutionary covariance, biochemistry and SAXS analyses reveal that Escherichia coli FliG exists as a monomer in solution but forms domain-swapped polymers in assembled flagellar motors, thus leading to a thermodynamic model for self-assembly.

CENP-C directs a structural transition of CENP-A nucleosomes mainly through sliding of DNA gyres   pp204 - 208
Samantha J Falk, Jaehyoun Lee, Nikolina Sekulic, Michael A Sennett, Tae-Hee Lee, Lee & Ben E Black
doi:10.1038/nsmb.3175
Single-molecule FRET data reveal that CENP-A alters nucleosome structure by facilitating lateral passing of the two DNA gyres; this change is reversed by the nonhistone centromere protein CENP-C.

A new MCM modification cycle regulates DNA replication initiation   pp209 - 216
Lei Wei and Xiaolan Zhao
doi:10.1038/nsmb.3173
Complementary biochemical and genetic analyses reveal that SUMOylation of the six subunits of the MCM2-7 DNA helicase inhibits CMG formation, thereby negatively regulating DNA replication initiation in budding yeast.

Structure of the eukaryotic replicative CMG helicase suggests a pumpjack motion for translocation   pp217 - 224
Zuanning Yuan, Lin Bai, Jingchuan Sun, Roxana Georgescu, Jun Liu, Michael E O'Donnell & Huilin Li
doi:10.1038/nsmb.3170
A 3.7- to 4.8-A cryo-EM structure of the yeast CMG complex resolves two Mcm2-7 helicase conformations that may drive complex translocation and reveals an Mcm5-subunit domain inserted into the central channel, thus supporting a steric-exclusion model of DNA unwinding.

A U1 snRNP-specific assembly pathway reveals the SMN complex as a versatile hub for RNP exchange   pp225 - 230
Byung Ran So, Lili Wan, Zhenxi Zhang, Pilong Li, Eric Babiash, Jingqi Duan, Ihab Younis & Gideon Dreyfuss
doi:10.1038/nsmb.3167
The higher abundance of U1 among snRNPs is explained by the identification of an additional mode of assembly: RBP U1-70K bridges pre-U1 to SMN-Gemin2-Sm, thus establishing a Gemin5-independent assembly pathway.

See also: News and Views by Mayerle & Guthrie

7SK-BAF axis controls pervasive transcription at enhancers   pp231 - 238
Ryan A Flynn, Brian T Do, Adam J Rubin, Eliezer Calo, Byron Lee, Hannes Kuchelmeister, Michael Rale, Ci Chu, Eric T Kool, Joanna Wysocka, Paul A Khavari & Howard Y Chang
doi:10.1038/nsmb.3176
In addition to controlling Pol II pausing at promoters, the small nuclear RNA 7SK inhibits transcription at enhancers and super enhancers by recruiting the chromatin-remodeling complex BAF

Super-resolution 3D tomography of interactions and competition in the nuclear pore complex   pp239 - 247
Jiong Ma, Alexander Goryaynov and Weidong Yang
doi:10.1038/nsmb.3174
Mapping the spatial distribution of interaction sites between FG nucleoporins and nuclear transport receptors within the native NPC through SPEED microscopy reveals the 3D configuration of the FG-nucleoporin barrier and competition among transport receptors.

Crystal structures reveal the molecular basis of ion translocation in sodium/proton antiporters   pp248 - 255
Mathieu Coincon, Povilas Uzdavinys, Emmanuel Nji, David L Dotson, Iven Winkelmann, Saba Abdul-Hussein, Alexander D Cameron, Oliver Beckstein & David Drew
doi:10.1038/nsmb.3164
New crystal structures of the NapA antiporter in both outward- and inward-facing conformations provide evidence for an elevator-like ion-translocation mechanism in sodium/proton exchangers.

See also: News and Views by Ryan & Vandenberg

The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism   pp256 - 263
Christopher Mulligan, Cristina Fenollar-Ferrer, Gabriel A Fitzgerald, Ariela Vergara-Jaque, Desirée Kaufmann, Yan Li, Lucy R Forrest & Joseph A Mindell
doi:10.1038/nsmb.3166
'Repeat swap' modeling of the outward-facing conformation and biochemical analyses show that the bacterial VcINDY symporter uses an elevator-type mechanism for substrate transport across the cell membrane.

See also: News and Views by Ryan & Vandenberg

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