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The FEBS Journal

Cover image for Vol. 281 Issue 6

March 2014

Volume 281, Issue 6

Pages i–iii, 1517–1715

  1. Front Cover

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Editor's Choice
    5. Original Articles
    6. Author index
    7. Table of Contents
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      Front Cover (page i)

      Version of Record online: 18 MAR 2014 | DOI: 10.1111/febs.12642

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      Illustration of proof that identifies metabolic states with optimal specific flux as elementary flux modes by M.T. Wortel et al. (pp. 1547–1555).

  2. Editorial Information

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Editor's Choice
    5. Original Articles
    6. Author index
    7. Table of Contents
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      Editorial Information (pages ii–iii)

      Version of Record online: 18 MAR 2014 | DOI: 10.1111/febs.12642_1

  3. Editor's Choice

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Editor's Choice
    5. Original Articles
    6. Author index
    7. Table of Contents
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      Binding mode of the activity-modulating C-terminal segment of NS2B to NS3 in the dengue virus NS2B–NS3 protease (pages 1517–1533)

      Laura de la Cruz, Wan-Na Chen, Bim Graham and Gottfried Otting

      Version of Record online: 12 FEB 2014 | DOI: 10.1111/febs.12729

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      Dengue virus protease (NS2B-NS3pro) is essential for dengue virus infection and is thus a target of therapeutic interest. Several X-ray structures with either open or closed conformations are known for this two-component protease. In this issue, Otting and co-workers nicely demonstrate, using pseudocontact shifts induced by different paramagnetic lanthanide ions attached at different sites, that the protease in solution predominantly assumes a closed conformation in the absence of inhibitors and that any open conformation is hardly populated. This work strongly supports the use of the closed conformation in the rational design of inhibitors.

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  4. Original Articles

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Editor's Choice
    5. Original Articles
    6. Author index
    7. Table of Contents
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      LDL receptor/lipoprotein recognition: endosomal weakening of ApoB and ApoE binding to the convex face of the LR5 repeat (pages 1534–1546)

      Juan Martínez-Oliván, Xabier Arias-Moreno, Adrián Velazquez-Campoy, Oscar Millet and Javier Sancho

      Version of Record online: 6 FEB 2014 | DOI: 10.1111/febs.12721

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      The fifth calcium-binding repeat of the LDL receptor, LR5, uses its hydrophilic convex face to bind both ApoB (at both site A and site B) and ApoE, the complexes being weakened at low [Ca2+] and low pH. Thus, endosomal conditions favour dissociation of LDLR/lipoprotein complexes. LDLR might chelate lipoproteins and enhance complex affinity by using more than one calcium-binding repeat.

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      Metabolic states with maximal specific rate carry flux through an elementary flux mode (pages 1547–1555)

      Meike T. Wortel, Han Peters, Josephus Hulshof , Bas Teusink and Frank J. Bruggeman

      Version of Record online: 12 FEB 2014 | DOI: 10.1111/febs.12722

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      How can metabolic networks be optimized for specific growth rate or product formation? We have unraveled which metabolic networks optimize specific rates, namely elementary flux modes (EFMs). This is rather surprising, because EFMs are defined by stoichiometry only, while specific rates are influenced by the kinetics. This result paves the way for optimization of kinetic models of genome-scale networks.

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      An immunomodulatory role for the Mycobacterium tuberculosis region of difference 1 locus proteins PE35 (Rv3872) and PPE68 (Rv3873) (pages 1556–1570)

      Bhavana Tiwari, Amarendranath Soory and Tirumalai R. Raghunand

      Version of Record online: 12 FEB 2014 | DOI: 10.1111/febs.12723

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      The pathogenesis of Mycobacterium tuberculosis (M.tb) involves the coordinate action of multiple bacillary components that modulate host immune responses to ensure its survival. Here, we demonstrate that the PE-PPE protein pair PE35 (Rv3872) – PPE68 (Rv3873) located in the region of difference (RD) 1, physically interact and play an immunomodulatory role in regulating the pathophysiology of M.tb.

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      SSTY proteins co-localize with the post-meiotic sex chromatin and interact with regulators of its expression (pages 1571–1584)

      Aurélie Comptour, Charlotte Moretti, Maria-Elisabetta Serrentino, Jana Auer, Côme Ialy-Radio, Monika A. Ward, Aminata Touré, Daniel Vaiman and Julie Cocquet

      Version of Record online: 13 FEB 2014 | DOI: 10.1111/febs.12724

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      Post-meiotic XY gene expression is timely controlled during sperm differentiation and, when deregulated, leads to male infertility. We identified a novel protein, SSTY, which could contribute to control XY gene expression in post-meiotic male gametes. Indeed, SSTY is specifically expressed during sperm differentiation, co-localizes with the post-meiotic sex chromatin, and interacts with known regulators of XY gene expression, SLY and SLX/SLXL1.

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      Vertebrate Acyl CoA synthetase family member 4 (ACSF4-U26) is a β-alanine-activating enzyme homologous to bacterial non-ribosomal peptide synthetase (pages 1585–1597)

      Jakub Drozak, Maria Veiga-da-Cunha, Beata Kadziolka and Emile Van Schaftingen

      Version of Record online: 12 FEB 2014 | DOI: 10.1111/febs.12725

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      ACSF4-U26, a conserved protein in eukaryotes, comprises an adenylation-domain, a phosphopantetheine group and a PQQDH-related domain. Mouse ACSF4-U26 loads its phosphopantetheine specifically with β-alanine. Its sluggishness, the absence of detectable β-alanine transfer onto small amines and the presence of a protein interaction domain lead us to speculate that ACSF4-U26 is involved in an unknown post-translational or post-transcriptional modification.

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      Crystal structure of mouse mu-crystallin complexed with NADPH and the T3 thyroid hormone (pages 1598–1612)

      Franck Borel, Isma Hachi, Andres Palencia, Marie-Claude Gaillard and Jean-Luc Ferrer

      Version of Record online: 10 FEB 2014 | DOI: 10.1111/febs.12726

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      We report the crystal structure of mouse Mu-crystallin under different states. This first description of the ternary complex, containing both NADPH and T3 allows the localization of the thyroid hormone binding site and a precise description of its binding mode. The kinetic parameters of the ligands and the specificity of the binding pocket were also investigated.

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      Allosteric regulation and substrate activation in cytosolic nucleotidase II from Legionella pneumophila (pages 1613–1628)

      Bharath Srinivasan, Farhad Forouhar, Arpit Shukla, Chethana Sampangi, Sonia Kulkarni, Mariam Abashidze, Jayaraman Seetharaman, Scott Lew, Lei Mao, Thomas B. Acton, Rong Xiao, John K. Everett, Gaetano T. Montelione, Liang Tong and Hemalatha Balaram

      Version of Record online: 17 FEB 2014 | DOI: 10.1111/febs.12727

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      Legionella pneumophila cytosolic nucleotidase II (LpcN-II) hydrolyzes GMP, dGMP and IMP. GTP, GDP and the substrate GMP allosterically modulate LpcN-II activity. Crystal structures of LpcN-II revealed an activator binding site at the dimer interface, further confirmed by site-directed mutagenesis. Structural changes induced in LpcN-II tetramer upon activator binding may be the molecular mechanism of activation.

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      Transcription factor C/EBP-β mediates downregulation of dipeptidyl-peptidase III expression by interleukin-6 in human glioblastoma cells (pages 1629–1641)

      Ratnakar Singh, Mehar C. Sharma, Chitra Sarkar, Manmohan Singh and Shyam S. Chauhan

      Version of Record online: 17 FEB 2014 | DOI: 10.1111/febs.12728

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      Expressions of DPP III (a cytosolic metallo-aminopeptidase implicated in various physiological and pathological processes) and IL-6 were studied in glioblastoma and found to exhibit a negative correlation. Investigating the role of IL-6 on DPP III expression revealed that this cytokine enhance the levels of C/EBP β which in turn transcriptionally down regulates DPP III expression.

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      Structural and kinetic studies on adenylosuccinate lyase from Mycobacterium smegmatis and Mycobacterium tuberculosis provide new insights on the catalytic residues of the enzyme (pages 1642–1658)

      Sanchari Banerjee, Monika J. Agrawal, Diptimayee Mishra, Siddharth Sharan, Hemalatha Balaram, Handanhal S. Savithri and Mathur R. N. Murthy

      Version of Record online: 20 FEB 2014 | DOI: 10.1111/febs.12730

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      X-ray crystal structure of Mycobacterium smegmatis apo-adenylosuccinate lyase (ASL) with a partially ordered active site loop was determined at 2.16 Å resolution. Comparative analysis of ASL structures suggests that His149, Lys285 and Ser279 are likely to be functionally important. The low catalytic activity observed for M. smegmatis and M. tuberculosis ASLs is consistent with their slow growth rate.

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      In vivo-folded metal–metallothionein 3 complexes reveal the Cu–thionein rather than Zn–thionein character of this brain-specific mammalian metallothionein (pages 1659–1678)

      Ester Artells, Òscar Palacios, Mercè Capdevila and Sílvia Atrian

      Version of Record online: 19 FEB 2014 | DOI: 10.1111/febs.12731

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      The Zn2+-, Cd2+- and Cu+-binding abilities of the mammalian brain-specific MT3 isoform were recombinantly investigated. MT3 accurately sensed different Cu contents in its synthesis environment, and it showed a peculiar dual ability to handle Zn2+ and Cu+ ions. Therefore, MT3 exhibits a Cu-thionein character stronger than MT1 and MT2, which are isoforms also present in the mammalian brain.

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      A secretory multifunctional serine protease, DegP of Plasmodium falciparum, plays an important role in thermo-oxidative stress, parasite growth and development (pages 1679–1699)

      Shweta Sharma, Mohit Jadli, Anu Singh, Kavita Arora and Pawan Malhotra

      Version of Record online: 24 FEB 2014 | DOI: 10.1111/febs.12732

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      Most pathogens, especially intracellular pathogens such as Plasmodium falciparum, encounter thermal and oxidative stresses during their establishment in host cells. Here, we show that PfDegP, a member of HtrA1 serine protease family, exists in complex with heat shock protein 70 (Hsp70), Fe-superoxide dismutase (FeSod) and enolase (Eno) and helps the parasite to combat these stresses.

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      Human steroid and oxysterol 7α-hydroxylase CYP7B1: substrate specificity, azole binding and misfolding of clinically relevant mutants (pages 1700–1713)

      Aleksei V. Yantsevich, Yaroslav V. Dichenko, Farrell MacKenzie, Dmitry V. Mukha, Alexander V. Baranovsky, Andrei A. Gilep, Sergey A. Usanov and Natallia V. Strushkevich

      Version of Record online: 20 FEB 2014 | DOI: 10.1111/febs.12733

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      Oxysterols and neurosteroids are important signaling molecules metabolized by cytochrome P450 CYP7B1, but its catalytic flexibility is not well understood. Substrate specificity, effect of disease-causing mutations and susceptibility to inhibition by azole antifungals were evaluated using enzymatic assays, mutagenesis and homology modeling. 21-hydroxypregnenolone was identified as a new substrate and additional metabolites were detected with oxysterols, expanding the CYP7B1 role.

  5. Author index

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Editor's Choice
    5. Original Articles
    6. Author index
    7. Table of Contents
    1. You have free access to this content
      Author index (page 1714)

      Version of Record online: 18 MAR 2014 | DOI: 10.1111/febs.12643

  6. Table of Contents

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Editor's Choice
    5. Original Articles
    6. Author index
    7. Table of Contents
    1. You have free access to this content
      Table of Contents (page 1715)

      Version of Record online: 18 MAR 2014 | DOI: 10.1111/febs.12644

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