• Issue
    Volume 20, Issue 7
    i-v, 543-624
    July 2015


Free Access

Issue Information

  • Pages: ii-v
  • First Published: 01 July 2015


Open Access

Protein monoubiquitylation: targets and diverse functions

  • Pages: 543-562
  • First Published: 18 June 2015
Description unavailable

Monoubiquitylation occurs more frequently than polyubiquitylation. Studies are beginning to provide insight into its biologically important functions.


Free Access

Discovery of an NRF1-specific inducer from a large-scale chemical library using a direct NRF1-protein monitoring system

  • Pages: 563-577
  • First Published: 04 May 2015
Description unavailable

To develop an NRF1-specific inducer which could be used to understand the role of NRF1 within the cell. We developed a novel NRF1▵C-Luc fusion protein probe and stably expressed cell-line, Hepa:N1▵C-Luc reporter system. Through HTS using this cell line, we have successfully identified the first small compound which specifically stabilizes NRF1.

Free Access

Heme-mediated inhibition of Bach1 regulates the liver specificity and transience of the Nrf2-dependent induction of zebrafish heme oxygenase 1

  • Pages: 590-600
  • First Published: 18 May 2015
Description unavailable

We previously showed the Nrf2-mediated induction of the zebrafish heme oxygenase 1 gene (hmox1a) to be liver-specific and transient. We herein identified that a factor governing this regulation is Bach1 (Bach1a and Bach1b in zebrafish) and heme mediates this regulation through Bach1 inhibition based on its level in each tissue.

Free Access

Cross talk in promoter recognition between six NarL-family response regulators of Escherichia coli two-component system

  • Pages: 601-612
  • First Published: 26 May 2015
Description unavailable

Cross talk of bacterial two-component system takes place at three stages: signal recognition by sensor kinase (stage-1); response regulator phosphorylation by sensor kinase (stage-2); and target recognition by response regulator (stage-3).

Free Access

Functional role of the C-terminal tail of the archaeal ribosomal stalk in recruitment of two elongation factors to the sarcin/ricin loop of 23S rRNA

  • Pages: 613-624
  • First Published: 02 June 2015
Description unavailable

Two types of elongation factors alternate in their binding to the factor-binding center of the ribosome. The multi-copy ribosomal protein family, termed the stalk, contributes actively to the factor recruitment. Our results suggest a crucial role for the interactions between the stalk C-terminal tail and elongation factors in their recruitment to the SRL of 23S rRNA within the ribosome.