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FEBS Journal

Cover image for Vol. 280 Issue 15

August 2013

Volume 280, Issue 15

Pages i–iii, 3483–3722

  1. Front Cover

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. MiniReview Series
    5. Minireview
    6. Minireview Series
    7. Minireview
    8. Original Articles
    9. Author index
    10. Table of Contents
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      Front Cover (page i)

      Article first published online: 17 JUL 2013 | DOI: 10.1111/j.1742-4658.2013.08788.x

      Thumbnail image of graphical abstract

      ARTD/PARP ADP-ribosylation proteins and tankyrase-mediated ADP-ribosylation in a slot-blot assay by Herwig Schüler & Mathias Ziegler (pp. 3542). (Background) Visualization of tankyrase-mediated ADP-ribosylation using biotin-NAD in a slot-blot assay format (E. Kuznetsowa & H. Schüler). (Main picture) Crystal structure of ARTD1/PARP1 bound to DNA (Langelier et al. (2012) Science 336, 728–732). Image created with PyMol using Protein Data Bank entry 4DQY. NAD was modeled into the active site by superimposition of the NAD-bound structure of Diphtheria toxin (PDB entry 1TOX). (left scheme) Overview of membrane-associated ecto-ART proteins (from S. Menzel et al., pp. 3543–3550). (right scheme) ARTD/PARP ADP-ribosylation cycle and ADP-ribose recognizing modules (from E. Barkauskaite et al., pp. 3491–3507).

  2. Editorial Information

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. MiniReview Series
    5. Minireview
    6. Minireview Series
    7. Minireview
    8. Original Articles
    9. Author index
    10. Table of Contents
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      Editorial Information (pages ii–iii)

      Article first published online: 17 JUL 2013 | DOI: 10.1111/j.1742-4658.2013.08788_1.x

  3. MiniReview Series

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. MiniReview Series
    5. Minireview
    6. Minireview Series
    7. Minireview
    8. Original Articles
    9. Author index
    10. Table of Contents
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      Physiology of ADP-ribosylation (page 3483)

      Friedrich Koch-Nolte and Mathias Ziegler

      Article first published online: 12 JUL 2013 | DOI: 10.1111/febs.12389

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      ADP-ribosylation of proteins is a versatile post-translational modification that can alter the chemistry of a specific side chain or provide a handle for the binding of a recognition domain. A better understanding of ADP-ribosylating enzymes and their targets is opening new therapeutic opportunities. This minireview series focuses on physiological aspects of ADP-ribosylation, while a companion series focuses on drug targets.

  4. Minireview

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. MiniReview Series
    5. Minireview
    6. Minireview Series
    7. Minireview
    8. Original Articles
    9. Author index
    10. Table of Contents
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      ADP-ribosylation, a mechanism regulating nitrogenase activity (pages 3484–3490)

      Stefan Nordlund and Martin Högbom

      Article first published online: 9 MAY 2013 | DOI: 10.1111/febs.12279

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      Nitrogen fixation is the vital biochemical process in which atmospheric molecular nitrogen is made available to the biosphere. The process is highly energetically costly and thus tightly regulated. The activity of the key enzyme, nitrogenase is controlled by reversible mono-ADP-ribosylation of one of its components. Here we review the current biochemical and structural knowledge of this central regulatory reaction.

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      The recognition and removal of cellular poly(ADP-ribose) signals (pages 3491–3507)

      Eva Barkauskaite, Gytis Jankevicius, Andreas G. Ladurner, Ivan Ahel and Gyula Timinszky

      Article first published online: 18 JUN 2013 | DOI: 10.1111/febs.12358

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      Poly(ADP-ribosyl)ation is an evolutionary conserved dynamic post-translational modification involved in a variety of biological functions. Poly(ADP-ribose) has a short half-life and the cellular levels of poly(ADP-ribose) are tightly regulated by both its production and degradation. In this review, we discuss the current knowledge of the protein modules that recognize poly(ADP-ribose) and summarize the newest developments on the degradation of poly(ADP-ribose).

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      The expanding role of PARPs in the establishment and maintenance of heterochromatin (pages 3508–3518)

      Françoise Dantzer and Raffaella Santoro

      Article first published online: 27 JUN 2013 | DOI: 10.1111/febs.12368

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      PARP1 and PARP2 are poly(ADP-ribose) polymerases (PARPs/ARTDs), enzymes that transfer poly(ADP-ribose) groups to target proteins and thereby affect cellular processes. The activity of PARP1 and PARP2 is tied to cellular signalling pathways, and through poly(ADP-ribosyl)ation they promote changes in chromatin architecture and gene expression. Here, we describe the role of PARPs in heterochromatin and their contribution in biological outcomes.

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      Expanding functions of intracellular resident mono-ADP-ribosylation in cell physiology (pages 3519–3529)

      Karla L. H. Feijs, Patricia Verheugd and Bernhard Lüscher

      Article first published online: 28 MAY 2013 | DOI: 10.1111/febs.12315

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      Mono-ADP-ribosylation is a post-translational modification, in which ADP-ribose is transferred from the cofactor NAD+ onto substrates by ADP-ribosyltransferases. Recent developments suggest that mono-ADP-ribosylation is a mechanism involved in controlling different signaling pathways, including NF-κB. Mono-ADP-ribosylation is read by certain macrodomain-containing proteins and removed by macrodomain-containing hydrolases. Together these novel findings establish mono-ADP-ribosylation as a reversible modification controlling different physiological pathways.

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      NAD and ADP-ribose metabolism in mitochondria (pages 3530–3541)

      Christian Dölle, Johannes G.M. Rack and Mathias Ziegler

      Article first published online: 3 JUN 2013 | DOI: 10.1111/febs.12304

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      NAD plays an essential role in mitochondria as redox cofactor and substrate for signalling reactions. NAD dependent signalling involves degradation of the nucleotide and conversion to ADP-ribose derivatives including second messenger generation and posttranslational protein modifications. The major NAD dependent reactions within mitochondria, their metabolic and regulatory function, and fate of NAD degradation products are highlighted.

  5. Minireview Series

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. MiniReview Series
    5. Minireview
    6. Minireview Series
    7. Minireview
    8. Original Articles
    9. Author index
    10. Table of Contents
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      Pharmacology of ADP-ribosylation (page 3542)

      Herwig Schüler and Mathias Ziegler

      Article first published online: 5 JUL 2013 | DOI: 10.1111/febs.12388

      Thumbnail image of graphical abstract

      ADP-ribosyltransferase ARTD1/PARP1 is a target for cancer and ischemia drug development. Several other ARTD-family enzymes have been characterized in recent years, and it has become clear that their inhibition might also have therapeutic value. This minireview series summarizes current knowledge of pharmacological inhibition of ADP-ribosyltransferases by a compound class called PARP inhibitors and the prospects for drug development.

  6. Minireview

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. MiniReview Series
    5. Minireview
    6. Minireview Series
    7. Minireview
    8. Original Articles
    9. Author index
    10. Table of Contents
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      The art of blocking ADP-ribosyltransferases (ARTs): Nanobodies as experimental and therapeutic tools to block mammalian and toxin ARTs (pages 3543–3550)

      Stephan Menzel, Björn Rissiek, Friedrich Haag, Fernando A. Goldbaum and Friedrich Koch-Nolte

      Article first published online: 14 JUN 2013 | DOI: 10.1111/febs.12313

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      Nanobodies, single domain antibodies derived from heavy-chain antibodies of llamas, are emerging as a promising new class of highly specific enzyme inhibitors. Here, we illustrate the potential of nanobodies as tools to block extracellular and intracellular ADP-ribosyltransferases using the toxin-related membrane-bound mammalian ecto-enzyme ARTC2 and the actin-ADP-ribosylating SpvB toxin of Salmonella entericae as examples.

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      A role of intracellular mono-ADP-ribosylation in cancer biology (pages 3551–3562)

      Emanuele S. Scarpa, Gaia Fabrizio and Maria Di Girolamo

      Article first published online: 10 MAY 2013 | DOI: 10.1111/febs.12290

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      A number of intracellular ARTD enzymes that are involved in the post-translational modification, mono-ADP-ribosylation, can have roles in cancer biology. The connection between cancer and ARTD8/PARP14 is well established. ARTD8, a Stat6-interacting protein, is associated with aggressiveness of B-cell lymphomas. The endoplasmic reticulum ARTD15/PARP16 can play a role in the nucleo-cytoplasmic trafficking. A dys-regulation of this process leads to the mislocalisation of oncogenic and tumour-suppressor proteins.

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      PARP inhibitors: polypharmacology versus selective inhibition (pages 3563–3575)

      Torun Ekblad, Emidio Camaioni, Herwig Schüler and Antonio Macchiarulo

      Article first published online: 24 MAY 2013 | DOI: 10.1111/febs.12298

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      PARP inhibitors have been a proof-of-concept showcase for the principle of synthetic lethality in cancer drug discovery. In this paper, we provide the reader with a historical perspective of existing PARP inhibitors in clinical trials, focusing on polypharmacology in contrast to selective inhibition, and providing an outlook on future directions in the field of design of selective inhibitors.

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      Tankyrases as drug targets (pages 3576–3593)

      Lari Lehtiö, Nai-Wen Chi and Stefan Krauss

      Article first published online: 18 JUN 2013 | DOI: 10.1111/febs.12320

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      This review describes the biochemical and cellular functions of the tankyrase subfamily of human ADP-ribosyltransferases. Tankyrases use NAD+ as a substrate to covalently modify acceptor proteins leading to dissociation of macromolecular complexes and protein degradation. Existing tankyrase inhibitors target the nicotinamide and/or the adenine pocket of the donor NAD+-binding cleft of the catalytic domain.

  7. Original Articles

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. MiniReview Series
    5. Minireview
    6. Minireview Series
    7. Minireview
    8. Original Articles
    9. Author index
    10. Table of Contents
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      Genes encoding 4-Cys antimicrobial peptides in wheat Triticum kiharae Dorof. et Migush.: multimodular structural organization, instraspecific variability, distribution and role in defence (pages 3594–3608)

      Lyubov L. Utkina, Yaroslav A. Andreev, Eugene A. Rogozhin, Tatyana V. Korostyleva, Anna A. Slavokhotova, Peter B. Oparin, Alexander A. Vassilevski, Eugene V. Grishin, Tsezi A. Egorov and Tatyana I. Odintsova

      Article first published online: 18 JUN 2013 | DOI: 10.1111/febs.12349

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      Genes encoded new wheat peptides code for precursor proteins of unusual multimodular structure consisting of a signal peptide, several α-hairpinin (4-Cys) peptide domains with a characteristic cysteine pattern separated by linkers and a C-terminal prodomain. Three types of precursor proteins, with five, six or seven 4-Cys peptide modules were found.

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      Nuclear factor-erythroid 2-related factor 1 regulates expression of proteasome genes in hepatocytes and protects against endoplasmic reticulum stress and steatosis in mice (pages 3609–3620)

      Candy S. Lee, Daniel V. Ho and Jefferson Y. Chan

      Article first published online: 18 JUN 2013 | DOI: 10.1111/febs.12350

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      Transcription factor Nrf1 regulates cellular stress response. In this study, we showed that Nrf1 regulates proteasome gene expression in the liver, and plays an integral role in the maintenance of proteasome function in hepatocytes and in the prevention of liver steatosis development. Our results also highlight an association between proteasome dysfunction, ER stress and steatosis.

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      Differences in oxygen-dependent nitric oxide metabolism by cytoglobin and myoglobin account for their differing functional roles (pages 3621–3631)

      Xiaoping Liu, Jianjing Tong, Joseph R. Zweier, Douglas Follmer, Craig Hemann, Raed S. Ismail and Jay L. Zweier

      Article first published online: 24 JUN 2013 | DOI: 10.1111/febs.12352

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      The rate of metCygb reduction by Asc is hundreds of times greater than the rate of metMb reduction by Asc. As a result, Cygb regulates the rate of NO catabolism in response to a change in oxygen concentration nearly 500 times more efficiently than Mb, enabling Cygb to efficiently regulate the oxygen-dependent NO metabolism in the vascular wall.

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      Cardiac glycosides correct aberrant splicing of IKBKAP-encoded mRNA in familial dysautonomia derived cells by suppressing expression of SRSF3 (pages 3632–3646)

      Bo Liu, Sylvia L. Anderson, Jinsong Qiu and Berish Y. Rubin

      Article first published online: 18 JUN 2013 | DOI: 10.1111/febs.12355

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      We report the ability of the cardiac glycoside digoxin to alter the splicing process and thereby increase production of the wild-type IKAP transcript in cells bearing the splice-altering familial dysautonomia (FD)-causing IKBKAP mutation. This digoxin-mediated effect is dependent on an SRSF3-binding site(s) located near the alternatively spliced exon and is the result of the digoxin-mediated suppression of the SRSF3 transcript and protein.

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      Human Drg1 is a potassium-dependent GTPase enhanced by Lerepo4 (pages 3647–3657)

      Isabel Pérez-Arellano, Mercedes Spínola-Amilibia and Jerónimo Bravo

      Article first published online: 24 JUN 2013 | DOI: 10.1111/febs.12356

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      Human Drg1 is regulated by Lerepo4. Its characterization demonstrates that potassium strongly stimulates its GTPase activity, without changing the monomeric status of Drg1. The Dfrp domain of Lerepo4 is the sole responsible for the Drg1 increase in thermal stability and the four fold stimulation over its catalytic activity. Lerepo4 action favors a switch I reorientation, mainly via the TGS domain.

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      Insulin-like growth factor-1 secreted by brain microvascular endothelial cells attenuates neuron injury upon ischemia (pages 3658–3668)

      Jun Wang, Yibo Tang, Wei Zhang, Haiping Zhao, Runjun Wang, Yangyang Yan, Liwei Xu and Pengtao Li

      Article first published online: 18 JUN 2013 | DOI: 10.1111/febs.12359

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      IGF-1 increased in serum and brain tissue, while IGFBP-2 decreased in brain tissue of MCAO rats. IGF-1 and IGFBP-2 expressions in primarily cultured were all significantly higher under OGD conditions in culture. IGF-1 administration improved the neuron viability upon normoxia or OGD, and upregulated p-Akt expression. Conditioned medium from OGD-induced BMECs substantially suppressed neuron viability and IGF-1R expression simultaneously.

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      pH modulates the binding of early growth response protein 1 transcription factor to DNA (pages 3669–3684)

      David C. Mikles, Vikas Bhat, Brett J. Schuchardt, Brian J. Deegan, Kenneth L. Seldeen, Caleb B. McDonald and Amjad Farooq

      Article first published online: 18 JUN 2013 | DOI: 10.1111/febs.12360

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      We show that the binding of EGR1 transcription factor to DNA is tightly regulated by solution pH by virtue of the ability of His382 to undergo protonation-deprotonation equilibrium. Remarkably, His382 is predominantly conserved across other members of EGR1 family, implying that histidine protonation-deprotonation may serve as a molecular switch for modulating protein-DNA interactions central to this family of transcription factors.

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      The ORF slr0091 of Synechocystis sp. PCC6803 encodes a high-light induced aldehyde dehydrogenase converting apocarotenals and alkanals (pages 3685–3696)

      Danika Trautmann, Peter Beyer and Salim Al-Babili

      Article first published online: 5 JUL 2013 | DOI: 10.1111/febs.12361

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      Aldehyde dehydrogenases play an important role in detoxification of reactive aldehydes. Here, we report on a cyanbacterial enzyme capable in converting two classes of lipid-derived aldehydes, apocaotenals and alkanals. The corresponding gene is a constituent of a stress-related operon, and homology to eukaryotic enzymes points to a yet not considered possibility of their being involved in scavenging of apocarotenals.

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      The Trichoderma atroviride photolyase-encoding gene is transcriptionally regulated by non-canonical light response elements (pages 3697–3708)

      Mayte G. Cervantes-Badillo, Tania Muñoz-Centeno, Edith E. Uresti-Rivera, Gerardo R. Argüello-Astorga and Sergio Casas-Flores

      Article first published online: 27 JUN 2013 | DOI: 10.1111/febs.12362

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      BLR-1 and BLR-2 integrate the BLR complex (BLRC), which is essential for phr-1 gene photoinduction in Trichoderma. We delimited a light responsive region (LRR) on the phr-1 promoter that contains non-canonical Light Response Elements compared to the light induced genes in Neurospora. Furthermore, the BLRC is located on the LRR in darkness ready to activate phr-1 in response to light.

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      Medicago truncatula histidine-containing phosphotransfer protein : Structural and biochemical insights into the cytokinin transduction pathway in plants (pages 3709–3720)

      Milosz Ruszkowski, Krzysztof Brzezinski, Robert Jedrzejczak, Miroslawa Dauter, Zbigniew Dauter, Michal Sikorski and Mariusz Jaskolski

      Article first published online: 24 JUN 2013 | DOI: 10.1111/febs.12363

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      The high-resolution crystal structure of Medicago truncatula histidine-containing phosphotransfer protein MtHPt1 reveals a helix bundle stabilized by S-aromatic interactions, with an exposed His79 residue that gets phosphorylated in a signal transduction cascade in plants that relays to the nucleus a signal elicited by a cytokinin molecule.

  8. Author index

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. MiniReview Series
    5. Minireview
    6. Minireview Series
    7. Minireview
    8. Original Articles
    9. Author index
    10. Table of Contents
    1. You have free access to this content
      Author index (page 3721)

      Article first published online: 17 JUL 2013 | DOI: 10.1111/j.1742-4658.2013.08787.x

  9. Table of Contents

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. MiniReview Series
    5. Minireview
    6. Minireview Series
    7. Minireview
    8. Original Articles
    9. Author index
    10. Table of Contents
    1. You have free access to this content
      Table of Contents (page 3722)

      Article first published online: 17 JUL 2013 | DOI: 10.1111/febs.12425

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