• Issue

    The FEBS Journal: Volume 283, Issue 16

    2965-3155
    August 2016

Issue Cover & Information

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Issue Cover & Information

  • Pages: 2965-2967
  • First Published: 19 August 2016
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Reimagining the cell – dissolving the boundaries of scientific specialisation by C. Kyne and P. Crowley (pp. 3016-3028). Permission to reproduce the image was kindly granted by Professor Adrian H. Elcock (University of Iowa, USA).

Editor's Choice

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Role of the yeast ribosomal protein L16 in ribosome biogenesis

  • Pages: 2968-2985
  • First Published: 04 July 2016
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Ribosomes are composed of two subunits – a large 60S subunit and small 40S subunit – each containing ribosomal RNA (rRNA) and proteins. Francisco Espinar-Marchena et al. characterise the contribution of the yeast 60S ribosomal protein L16 to ribosome biogenesis. They report that L16 assembles very early within nascent 60S ribosomal subunits and is required for the subsequent accumulation of 60S subunits in yeast. L16 is also shown to have an essential role in 27S pre-rRNA processing. The eukaryote-specific C-terminal extension of L16 facilitates pre-60S assembly but is not strictly essential for 27S pre-rRNA maturation.

Research Highlights

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Research Highlights

  • Pages: 2986
  • First Published: 05 August 2016
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In this issue, we highlight a report by Hiraoka et al. that provides insight into the signalling pathways that regulate the transition from meiotic prophase I to metaphase I; work by Franco et al. that shows how communication between clonal cancer cells promotes tumour growth; and a study by Zhang, Aubert et al. that identifies a core NuRD chromatin remodelling complex.

State-of-the-Art Review

Open Access

AMP-activated protein kinase: a cellular energy sensor that comes in 12 flavours

  • Pages: 2987-3001
  • First Published: 02 March 2016
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The two rounds of whole genome duplication that occurred during early vertebrate evolution produced two or three isoforms of each subunit of AMP-activated protein kinase (AMPK), generating up to twelve heterotrimeric combinations in mammals. These were thought to be rather similar in function, but recent evidence suggests that while some combinations may act as tumour suppressors, others may be oncogenes.

Review Article

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The JAK/STAT pathway in obesity and diabetes

  • Pages: 3002-3015
  • First Published: 12 March 2016
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The knowledge accumulated in recent years enable us to describe the mechanisms by which different subcomponents of the JAK-STAT signalling influence metabolic physiology, i.e. acting as regulators of food intake, liver steatosis, or immune-mediated pancreatic β-cell dysfunction and death. In this review, the “metabolic function” of JAK-STAT proteins is discussed in depth and the role of these molecules in different cell types compared.

Viewpoint

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Grasping the nature of the cell interior: from Physiological Chemistry to Chemical Biology

  • Pages: 3016-3028
  • First Published: 19 April 2016
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A major goal of biochemistry is to capture the molecular (re)arrangements that define functional regions in cells. Starting with the principles established by natural philosophers, we trace the discoveries that have shaped this current grand challenge. Important lessons are extracted for today's bioinspired scientists. The need for harmonised experimental practices and theoretical frameworks is considered as an alternative to intensive compartmentalisation. Future experiments and model systems are presented.

Original Articles

Open Access

Comprehensive characterization of ligand-induced plasticity changes in a dimeric enzyme

  • Pages: 3029-3038
  • First Published: 22 June 2016
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This study reports the first apo X-ray crystal structure of the antibiotic resistance enzyme AAC(6′)-Ii, and utilizes small-angle X-ray scattering and circular dichroism to characterize the inherent structural plasticity and ligand binding-induced conformational changes. These structural analyses provide insight into allosteric cooperativity of ligand binding.

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The crystal structure of the ligand-binding region of serine-glutamate repeat containing protein A (SgrA) of Enterococcus faecium reveals a new protein fold: functional characterization and insights into its adhesion function

  • Pages: 3039-3055
  • First Published: 23 June 2016
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SgrA is a surface protein of Enterococcus faecium implicated in binding to fibrinogen, nidogen, and abiotic surfaces. Here, we report the crystal structure of the ligand-binding domain of SgrA (rSgrA28–153). The structure revealed a new protein fold and contains a putative isopeptide bond. Even in the absence of isopeptide bond, rSgrA28–153 is resistant to proteases and exhibits high thermal stability. The surface-exposed hydrophobic patches likely play a significant role in the adhesion of SgrA toward abiotic surfaces, and this structural information could be useful to understand the role of SgrA in biofilm formation.

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The multiple stress responsive transcriptional regulator Rv3334 of Mycobacterium tuberculosis is an autorepressor and a positive regulator of kstR

  • Pages: 3056-3071
  • First Published: 23 June 2016
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Under aerobic condition, Rv3334 of M. tuberculosis acts as an autorepressor and prevents its own transcription by binding to a palindrome in its promoter. During hypoxia, the autorepression is relieved and the expressed Rv3334 protein binds to the promoter of KstR, the key regulator of lipid catabolism which has a similar palindrome, and activates its expression.

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Structural and functional characterization of the microtubule interacting and trafficking domains of two oomycete chitin synthases

  • Pages: 3072-3088
  • First Published: 01 July 2016
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Microtubule interacting and trafficking (MIT) domains do not typically occur in carbohydrate synthases, aside from some oomycete chitin synthases. We have characterized the MIT domains from two oomycete chitin synthases and show their interaction with the membrane component phosphatidic acid. We have solved the NMR structure of one of these domains and propose a structural model for a second MIT domain.

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Solution structure of the microtubule-targeting COS domain of MID1

  • Pages: 3089-3102
  • First Published: 01 July 2016
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Human MID1 is a microtubule-associated E3 ligase required for the development of the midline region during embryogenesis. We solved the NMR structures of a 60-amino acid COS box/domain found at the C-terminal end of the coiled-coil (CC) domain and showed that it adopts a helical structure and interacts with the CC domain to form a microtubule-binding spectrin-like fold. Binding studies confirmed direct interaction with the microtubules.

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Protein folding on biosensor tips: folding of maltodextrin glucosidase monitored by its interactions with GroEL

  • Pages: 3103-3114
  • First Published: 01 July 2016
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Chaperonin-based detection method on bio-layer interferometry can identify superior refolding conditions for denatured proteins. The degree of protein folding can be detected by monitoring the binding of chaperonin GroEL to the immobilized protein. GroEL interacts with proteins that have hydrophobic surfaces exposed in their unfolded/ partially folded states. The magnitude of GroEL binding inversely reflects the extent of protein folding.

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Gene signatures of estrogen and progesterone receptor pathways predict the prognosis of colorectal cancer

  • Pages: 3115-3133
  • First Published: 04 July 2016
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To clarify the controversial associations of ER and PR pathways with the prognosis of CRC, a novel gene signature-based approach was employed to semiquantitate the activities of these two pathways in CRC samples. The results indicate that the down-regulation of these two pathways, especially ER pathway, is common in CRC and significantly associated with recurrence risk of this cancer.

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The flexibility of a homeodomain transcription factor heterodimer and its allosteric regulation by DNA binding

  • Pages: 3134-3154
  • First Published: 08 July 2016
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Transcription factors can modify the shape of DNA; however, DNA can also serve as an allosteric ligand that changes the conformation of transcriptional regulators. We demonstrate through a number of biochemical and biophysical methods that the heterodimer PBX1:PREP1, that plays major roles in embryonic development and tumorigenesis, exhibits a structural change upon DNA binding. These changes provide important insights to determine how PBX1:PREP1 heterodimer functions.

Table of Contents

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Table of Contents

  • Pages: 3155
  • First Published: 19 August 2016