Thursday, September 7, 2017

Nature Structural & Molecular Biology Contents: 2017 Volume #24 pp 683 - 782

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TABLE OF CONTENTS

September 2017 Volume 24, Issue 9

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News and Views

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Identification of an allosteric network that influences assembly and function of group II chaperonins   pp683 - 684
Mingliang Jin and Yao Cong
doi:10.1038/nsmb.3459
Group II chaperonins facilitate protein folding by undergoing ATP-driven conformational changes. A recent study reveals a tunable allosteric network in group II chaperonins that includes a residue at the intersubunit interface, which is important for assembly and allosteric coordination. The authors also propose that lower cooperativity allows group II chaperonins to achieve optimal substrate folding over a broad range of ATP concentrations.

See also: Article by Lopez et al.

Oocyte-derived histone H3 lysine 27 methylation controls gene expression in the early embryo   pp685 - 686
Rakesh Pathak and Robert Feil
doi:10.1038/nsmb.3456
The monoallelic expression of many imprinted genes in mammals depends on DNA methylation marks that originate from the germ cells. Recent studies in mice and fruit flies evoke a novel, transient mode of genomic imprinting in which oocyte-acquired histone H3 Lys27 trimethylation (H3K27me3) marks are transmitted to the zygote and modulate the allele specificity and timing of gene expression in the early embryo.
 

Aging: rewiring the circadian clock   pp687 - 688
Rika Ohkubo and Danica Chen
doi:10.1038/nsmb.3461
The robustness of the circadian clock deteriorates with aging. Two new studies show that aging reprograms the circadian transcriptome in a cell-type-dependent manner and that such rewiring can be reversed by caloric restriction.
 

A tripartite interface that regulates vesicle fusion   p688
Ines Chen
doi:10.1038/nsmb.3468
 

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Review

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Eukaryotic ribosome assembly, transport and quality control   pp689 - 699
Cohue Pena, Ed Hurt and Vikram Govind Panse
doi:10.1038/nsmb.3454
In this Review, Pena, Hurt and Panse discuss our current knowledge on the eukaryotic ribosome assembly, a complex process that takes place across different cellular compartments and involves over 200 assembly factors.
 

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Rps26 directs mRNA-specific translation by recognition of Kozak sequence elements   pp700 - 707
Max B Ferretti, Homa Ghalei, Ethan A Ward, Elizabeth L Potts and Katrin Karbstein
doi:10.1038/nsmb.3442
Rps26 promotes translation by recognition of the Kozak sequence in well-translated mRNAs, whereas exposure to cellular stress leads to formation of Rps26-deficient ribosomes, which preferentially translate stress-response mRNAs with Kozak sequence deviations.
 

Decoding the selectivity of eIF2α holophosphatases and PPP1R15A inhibitors   pp708 - 716
Marta Carrara, Anna Sigurdardottir and Anne Bertolotti
doi:10.1038/nsmb.3443
The activities of human holophosphatases R15A-PP1 and R15B-PP1 on substrate eIF2α are now reconstituted in vitro, revealing that inhibitors Guanabenz and Sephin1 induce a selective conformational change in R15A and impair the recruitment of eIF2α.
 

Katanin spiral and ring structures shed light on power stroke for microtubule severing   pp717 - 725
Elena Zehr, Agnieszka Szyk, Grzegorz Piszczek, Ewa Szczesna, Xiaobing Zuo et al.
doi:10.1038/nsmb.3448
Using a combination of crystallography, SAXS and cryo-EM, the katanin hexamer is observed in spiral or ring arrangements, suggesting a mechanism to generate the power stroke to severe microtubules.
 

An information theoretic framework reveals a tunable allosteric network in group II chaperonins   pp726 - 733
Tom Lopez, Kevin Dalton, Anthony Tomlinson, Vijay Pande and Judith Frydman
doi:10.1038/nsmb.3440
Identification of a tunable network of covarying residues within group II chaperonins suggests how these proteins support robust folding of their clients over a wide range of metabolic conditions.

See also: News and Views by Jin & Cong

TRF2 binds branched DNA to safeguard telomere integrity   pp734 - 742
Isabelle Schmutz, Leonid Timashev, Wei Xie, Dinshaw J Patel and Titia de Lange
doi:10.1038/nsmb.3451
Functional analysis of TRF2-RuvC chimeras establishes that binding of the TRF2 basic domain to branched-DNA structures of the t-loop is responsible for telomere protection in mouse and human cells.
 

Structural basis of TIR-domain-assembly formation in MAL- and MyD88-dependent TLR4 signaling   pp743 - 751
Thomas Ve, Parimala R Vajjhala, Andrew Hedger, Tristan Croll, Frank DiMaio et al.
doi:10.1038/nsmb.3444
Structural insight into TIR-domain interactions, which are essential for the recruitment of signaling adapters to Toll-like receptors during innate immune responses, demonstrates a conserved interaction mode involved in both TLR and IL-1R signaling.
 

An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome   pp752 - 757
Tanja Florin, Cristina Maracci, Michael Graf, Prajwal Karki, Dorota Klepacki et al.
doi:10.1038/nsmb.3439
Antimicrobial peptide Api137 inhibits translation by trapping release factors 1 or 2 associated with ribosomes and arresting termination.
 

X-ray structures of endothelin ETB receptor bound to clinical antagonist bosentan and its analog   pp758 - 764
Wataru Shihoya, Tomohiro Nishizawa, Keitaro Yamashita, Asuka Inoue, Kunio Hirata et al.
doi:10.1038/nsmb.3450
Crystal structures of human endothelin ETB receptor bound to bosentan and to ETB-selective derivative provide insight into the basis of antagonism by these drugs.
 

Constraints and consequences of the emergence of amino acid repeats in eukaryotic proteins   pp765 - 777
Sreenivas Chavali, Pavithra L Chavali, Guilhem Chalancon, Natalia Sanchez de Groot, Rita Gemayel et al.
doi:10.1038/nsmb.3441
Computational analyses of the yeast proteome and experimental work show that homorepeats facilitate protein-protein interactions and rapid protein divergence. To balance their propensity to aggregate, homorepeats are preferentially retained in proteins that are stringently regulated.
 

Hydroxylation of a conserved tRNA modification establishes non-universal genetic code in echinoderm mitochondria   pp778 - 782
Asuteka Nagao, Mitsuhiro Ohara, Kenjyo Miyauchi, Shin-ichi Yokobori, Akihiko Yamagishi et al.
doi:10.1038/nsmb.3449
In echinoderm mitochondria, the codon AAA encodes asparagine instead of lysine. A newly identified nucleoside modification, hydroxy-N6-threonylcarbamoyladenosine (ht6A), is found adjacent to the anticodon in mt-tRNALys and prevents mt-tRNALys from misreading AAA as lysine.
 

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