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TABLE OF CONTENTS
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| September 2017 Volume 24, Issue 9 |
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News and Views | Top |
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Review | Top |
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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. |
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| 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. |
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| 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. |
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| 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 |
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| 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. |
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| 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. |
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| 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. |
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| 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. |
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| 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. |
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| 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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