FEBS Letters
Volume 582, Issue 29 , Pages 3991-3996, 10 December 2008

Thiamin-dependent transactivation activity of PDC2 in Saccharomyces cerevisiae

Edited by Judit Ovádi

  • Kazuto Nosaka

      Affiliations

    • Department of Chemistry, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kita-ku, Kyoto 603-8334, Japan
    • Corresponding Author InformationCorresponding author. Fax: +81 75 465 7651.
  • ,
  • Mari Onozuka

      Affiliations

    • Department of Radioisotope Laboratory, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kamigyo-ku, Kyoto 602-8566, Japan
  • ,
  • Hiroyuki Konno

      Affiliations

    • Department of Chemistry, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kita-ku, Kyoto 603-8334, Japan
  • ,
  • Kenichi Akaji

      Affiliations

    • Department of Chemistry, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kita-ku, Kyoto 603-8334, Japan

Received 27 August 2008; received in revised form 4 October 2008; accepted 25 October 2008. published online 13 November 2008.

Abstract 

Yeast genes involved in thiamin pyrophosphate (TPP) synthesis are transcriptionally induced in response to thiamin starvation. In this system, three proteins (Thi2p, Thi3p, and Pdc2p) act as positive regulatory factors. Thi3p is a TPP-binding protein and upregulates THI genes expression when TPP is not bound. We found here that Pdc2p could transactivate gene expression and interact with Thi3p, both of which were enhanced by thiamin starvation. This enhancement of the transactivation activity was not observed in a thi3 strain. When the C-terminal region containing the deduced Thi3p-interacting domain was truncated, Pdc2p expressed striking transactivation activity in a Thi3p-independent fashion. We explored the hypothesis that Thi3p causes a conformational change in Pdc2p leading to full transactivation activity under favorable conditions.

Structured summary


MINT-6797334, MINT-6797355:

THI3 (uniprotkb:Q07471) physically interacts (MI:0218) with PDC2 (uniprotkb:P32896) by two hybrid (MI:0018)

MINT-6797316:

THI3 (uniprotkb:Q07471) physically interacts (MI:0218) with THI2 (uniprotkb:P38141) by two hybrid (MI:0018)

MINT-6797373:

THI3 (uniprotkb:Q07471) binds (MI:0407) to PDC2 (uniprotkb:P32896) by pull down (MI:0096)

Abbreviation: TPP, thiamin pyrophosphate

Keywords: Thiamin pyrophosphate, Transcriptional regulation, PDC2, THI3, Saccharomyces cerevisiae

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PII: S0014-5793(08)00899-5

doi:10.1016/j.febslet.2008.10.051

FEBS Letters
Volume 582, Issue 29 , Pages 3991-3996, 10 December 2008