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The EMBO Journal

Cover image for Vol. 30 Issue 14

July 20, 2011

Volume 30, Issue 14

Pages 2751–2982

  1. Have you seen?

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      How to split up: lessons from mitochondria (pages 2751–2753)

      Daniel Dikov and Andreas S Reichert

      Article first published online: 20 JUL 2011 | DOI: 10.1038/emboj.2011.219

      Mitochondria underlie a continuous cycle of fission and fusion. Recent studies published in The EMBO Journal, EMBO Reports and The Journal of Cell Biology identified factors that recruit the fission factor Drp1 to mitochondria and inhibit or activate Drp1 activity.

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      Tonight, the same old, deadly programme: BH3-only proteins, mitochondria and yeast (pages 2754–2756)

      Bjorn Oettinghaus, Stephan Frank and Luca Scorrano

      Article first published online: 20 JUL 2011 | DOI: 10.1038/emboj.2011.220

      According to the common belief, yeast lacks the key regulators of mitochondria-dependent apoptosis, Bcl-2 family members. This view is now challenged by the identification of a proapoptotic ‘BH3-only’ Bcl-2 family member, yeast Ybh3p.

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      Policing Parkin with a UblD (pages 2757–2758)

      Fen Liu and Kylie J Walters

      Article first published online: 20 JUL 2011 | DOI: 10.1038/emboj.2011.223

      Parkin, a ubiquitin ligase of the RING-IBR-RING family, is mutated in familial Parkinsonism. Exciting recent reports transform our thinking of its catalytic activity, and reveal a new autoinhibitory mechanism that is abolished by disease mutations

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      A mad partner for Shugoshin in meiosis (pages 2759–2761)

      Hongtao Yu

      Article first published online: 20 JUL 2011 | DOI: 10.1038/emboj.2011.217

      The centromeric cohesin protector Shugoshin (Sgo) and the spindle checkpoint protein Mad2 are known to act in distinct pathways for ensuring accurate chromosome segregation during eukaryotic cell division. A study in this issue of The EMBO Journal describes an unexpected physical interaction between vertebrate Sgo and Mad2, and hints to their potential mutual regulation in meiosis.

  2. Article

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      Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission (pages 2762–2778)

      Jian Zhao, Tong Liu, Shaobo Jin, Xinming Wang, Mingqi Qu, Per Uhlén, Nikolay Tomilin, Oleg Shupliakov, Urban Lendahl and Monica Nistér

      Article first published online: 24 JUN 2011 | DOI: 10.1038/emboj.2011.198

      Mitochondrial morphology depends on the balance between fission and fusion events. This study identifies a receptor for the fission factor Drp1 within the mitochondrial outer membrane, which inhibits Drp1-mediated fission and activates fusion.

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      A yeast BH3-only protein mediates the mitochondrial pathway of apoptosis (pages 2779–2792)

      Sabrina Büttner, Doris Ruli, F-Nora Vögtle, Lorenzo Galluzzi, Barbara Moitzi, Tobias Eisenberg, Oliver Kepp, Lukas Habernig, Didac Carmona-Gutierrez, Patrick Rockenfeller, Peter Laun, Michael Breitenbach, Chamel Khoury, Kai-Uwe Fröhlich, Gerald Rechberger, Chris Meisinger, Guido Kroemer and Frank Madeo

      Article first published online: 14 JUN 2011 | DOI: 10.1038/emboj.2011.197

      It has been assumed so far that yeast is devoid of BCL-2 family members. This study identifies the yeast BCL-2 homology domain 3 protein Ybh3p that triggers an intrinsic cell death pathway involving the mitochondrial phosphate carrier Mir1p.

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      A synthetic prestin reveals protein domains and molecular operation of outer hair cell piezoelectricity (pages 2793–2804)

      Thorsten J Schaechinger, Dmitry Gorbunov, Christian R Halaszovich, Tobias Moser, Sebastian Kügler, Bernd Fakler and Dominik Oliver

      Article first published online: 24 JUN 2011 | DOI: 10.1038/emboj.2011.202

      Prestin is an anion exchanger required for electromotility of the outer hair cells of the inner ear. This study characterizes the structural and functional basis for the piezoelectric properties of prestin that mediate electromotility.

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      The Sm-like RNA chaperone Hfq mediates transcription antitermination at Rho-dependent terminators (pages 2805–2816)

      Makhlouf Rabhi, Olivier Espéli, Annie Schwartz, Bastien Cayrol, A Rachid Rahmouni, Véronique Arluison and Marc Boudvillain

      Article first published online: 14 JUN 2011 | DOI: 10.1038/emboj.2011.192

      The RNA chaperone Hfq is known to play a role in regulatory small RNA function in bacteria. However, here Hfq is also described to be involved in Rho-dependent transcription termination.

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      Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase with role in transcription (pages 2817–2828)

      M Behfar Ardehali, Amanda Mei, Katie L Zobeck, Matthieu Caron, John T Lis and Thomas Kusch

      Article first published online: 21 JUN 2011 | DOI: 10.1038/emboj.2011.194

      Histone H3 lysine 4 trimethylation is a major hallmark of promoter-proximal histones at transcribed genes. In this study, the Drosophila Set1 methyltransferase is shown to be the enzyme predominantly responsible for this modification and involved in controlling the rate of RNA polymerase II release into productive elongation.

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      Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation (pages 2829–2842)

      Chuanbing Bian, Chao Xu, Jianbin Ruan, Kenneth K Lee, Tara L Burke, Wolfram Tempel, Dalia Barsyte, Jing Li, Minhao Wu, Bo O Zhou, Brian E Fleharty, Ariel Paulson, Abdellah Allali-Hassani, Jin-Qiu Zhou, Georges Mer, Patrick A Grant, Jerry L Workman, Jianye Zang and Jinrong Min

      Article first published online: 17 JUN 2011 | DOI: 10.1038/emboj.2011.193

      The SAGA complex is a large histone acetyltransferase complex. Here, the crystal structure of the Sgf29 subunits tandem Tudor domains demonstrates how Sgf29 recognizes methylated H3K4 to recruit the SAGA complex to its targets sites and mediate histone H3 acetylation.

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      Tra1 has specific regulatory roles, rather than global functions, within the SAGA co-activator complex (pages 2843–2852)

      Dominique Helmlinger, Samuel Marguerat, Judit Villén, Danielle L Swaney, Steven P Gygi, Jürg Bähler and Fred Winston

      Article first published online: 3 JUN 2011 | DOI: 10.1038/emboj.2011.181

      The SAGA complex is a conserved, multifunctional co-activator that is thought to have a broad role in eukaryotic transcription. Here, systematic genetic and gene expression analysis identifies more specific regulatory functions of individual SAGA subunits than previously anticipated.

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      Autoregulation of Parkin activity through its ubiquitin-like domain (pages 2853–2867)

      Viduth K Chaugule, Lynn Burchell, Kathryn R Barber, Ateesh Sidhu, Simon J Leslie, Gary S Shaw and Helen Walden

      Article first published online: 21 JUN 2011 | DOI: 10.1038/emboj.2011.204

      Despite Parkin's key roles in mitophagy and Parkinson's disease pathology, its molecular function as ubiquitin ligase have remained ill defined. The key may be intramolecular autoinhibition of its E3 activity, a regulatory mechanism that is disrupted by disease mutation.

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      Shugoshin is a Mad1/Cdc20-like interactor of Mad2 (pages 2868–2880)

      Michael Orth, Bernd Mayer, Kinga Rehm, Ulli Rothweiler, Doris Heidmann, Tad A Holak and Olaf Stemmann

      Article first published online: 10 JUN 2011 | DOI: 10.1038/emboj.2011.187

      The checkpoint protein Mad2 binds both its activator Mad1 and its target Cdc20 via a peculiar ‘safety belt’ conformation. The unexpected finding of a similar highly specific interaction with the mammalian meiotic cohesin protector Sgo2 suggests a new link between chromosome segregation and the spindle assembly checkpoint.

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      Atomic force microscopy captures MutS tetramers initiating DNA mismatch repair (pages 2881–2893)

      Yong Jiang and Piotr E Marszalek

      Article first published online: 10 JUN 2011 | DOI: 10.1038/emboj.2011.180

      DNA mismatch repair requires long-distance communication between damage and incision sites. Direct observation of the MutS mismatch detection protein may reconcile the present ‘sliding’ and ‘looping’ models, by suggesting cooperation of non-equivalent MutS dimers: one dimer remains mismatch immobilized, while its associated partner moves on DNA to reel in loops.

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      Modulation of Tcf3 repressor complex composition regulates cdx4 expression in zebrafish (pages 2894–2907)

      Hyunju Ro and Igor B Dawid

      Article first published online: 10 JUN 2011 | DOI: 10.1038/emboj.2011.184

      Here, E4f1 is identified as a regulator of Tcf3 activity: causing dissociation of corepressor factors and thus promoting Tcf3's transcriptional activator function. E4f1 is important for Tcf3-mediated induction of Cdx4 during zebrafish development.

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      An autism-associated point mutation in the neuroligin cytoplasmic tail selectively impairs AMPA receptor-mediated synaptic transmission in hippocampus (pages 2908–2919)

      Mark R Etherton, Katsuhiko Tabuchi, Manu Sharma, Jaewon Ko and Thomas C Südhof

      Article first published online: 3 JUN 2011 | DOI: 10.1038/emboj.2011.182

      The autism-associated point mutation R704C targets a conserved arginine residue in the cytoplasmic sequence of neuroligin-4. This mutation, when introduced into neuroligin-3, leads to major changes in synaptic transmission in excitatory synapses, supporting that the cytoplasmic tail of neuroligin-3 has an important role in synaptic transmission.

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      FLRT2 and FLRT3 act as repulsive guidance cues for Unc5-positive neurons (pages 2920–2933)

      Satoru Yamagishi, Falko Hampel, Katsuhiko Hata, Daniel del Toro, Manuela Schwark, Elena Kvachnina, Martin Bastmeyer, Toshihide Yamashita, Victor Tarabykin, Rüdiger Klein and Joaquim Egea

      Article first published online: 14 JUN 2011 | DOI: 10.1038/emboj.2011.189

      The Unc5 receptor binds to fibronectin and leucine-rich transmembrane protein family members (FLRT). FLRT2/3 ectodomains are shed from neurons by proteolysis to generate diffusible repulsive guidance molecules for Unc5-expressing neurons

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      Identity, regulation and in vivo function of gut NKp46+RORγt+ and NKp46+RORγt lymphoid cells (pages 2934–2947)

      Ana Reynders, Nadia Yessaad, Thien-Phong Vu Manh, Marc Dalod, Aurore Fenis, Camille Aubry, Georgios Nikitas, Bertrand Escalière, Jean Christophe Renauld, Olivier Dussurget, Pascale Cossart, Marc Lecuit, Eric Vivier and Elena Tomasello

      Article first published online: 17 JUN 2011 | DOI: 10.1038/emboj.2011.201

      Gut NKp46+RORγt+ and NKp46+RORγt lymphoid cells contribute to early immune responses in mucosal tissues. The findings report here on the lineage relationship and function of these two subsets and their role in host defence against the enteric pathogen L. monocytogenes.

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      An infrequent molecular ruler controls flagellar hook length in Salmonella enterica (pages 2948–2961)

      Marc Erhardt, Hanna M Singer, Daniel H Wee, James P Keener and Kelly T Hughes

      Article first published online: 7 JUN 2011 | DOI: 10.1038/emboj.2011.185

      The bacterial flagellum is connected to the cell surface by the hook, a structure of defined length. This study takes the modelling approaches to understand how hook length is regulated by the secreted protein FliK.

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      Architecture of the flagellar rotor (pages 2962–2971)

      Koushik Paul, Gabriela Gonzalez-Bonet, Alexandrine M Bilwes, Brian R Crane and David Blair

      Article first published online: 14 JUN 2011 | DOI: 10.1038/emboj.2011.188

      Structural analysis of the bacterial flagellar rotor proteins FliG and FliM provides insight into the assembly of this complex structure, and into the mechanisms underlying motor rotation.

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      Structural diversity of bacterial flagellar motors (pages 2972–2981)

      Songye Chen, Morgan Beeby, Gavin E Murphy, Jared R Leadbetter, David R Hendrixson, Ariane Briegel, Zhuo Li, Jian Shi, Elitza I Tocheva, Axel Müller, Megan J Dobro and Grant J Jensen

      Article first published online: 14 JUN 2011 | DOI: 10.1038/emboj.2011.186

      A comprehensive electron cryotomographical survey of bacterial flagellar motors reveals the existence of a conserved structural core that is surrounded by a divergent set of novel structural features. Key proteins of the flagellar export apparatus can now be localized within the motor.

  3. Corrigendum

    1. Top of page
    2. Have you seen?
    3. Article
    4. Corrigendum
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      The nuclear RNA polymerase II surveillance system targets polymerase III transcripts (page 2982)

      Wiebke Wlotzka, Grzegorz Kudla, Sander Granneman and David Tollervey

      Article first published online: 20 JUL 2011 | DOI: 10.1038/emboj.2011.209

      This article corrects:

      The nuclear RNA polymerase II surveillance system targets polymerase III transcripts

      Vol. 30, Issue 9, 1790–1803, Article first published online: 1 APR 2011

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