Dissecting functional domains in the cation stress response transcription factor SltA

Author:

Elena Requena, Ana M. Alonso, Eduardo A. Espeso

Author address:

Department of Cellular and Molecular Biology, Centro de Investigaciones Biológicas (CSIC), Madrid, Spain

Full conference title:

15th European Conference on Fungal Genetics 2020

Date: 20 June 2020

Abstract:

A proper response to elevated extracellular concentrations of mono and divalent cations and alkalinity require the activity of the zinc finger transcription factor SltA in Aspergillus nidulans. As the well-known transcription factor PacC mediating ambient pH response, SltA is activated by proteolytic processing. The serine protease SltB cleaves the primary 78 kDa form of SltA to render the functional 32 kDa version. SltA 32 kDa comprises the DNA binding domain plus a very poorly conserved C-terminal region among homologues. In this work we have focused on the identification of proteolytic determinants and the nuclear transport signals in SltA. We found several nuclear localization signals along the SltA32kDa form, the need of SltA proteolysis for its nuclear localization and the cleavage site for SltB protease.

Link to conference website:

Link Conference abstract: 

ECFG 15

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