Plant Transcription Factor Database
Previous version: v3.0
Brachypodium stacei
HSF Family
Species TF ID Description
Brast01G146300.1.pHSF family protein
Brast01G155400.1.pHSF family protein
Brast01G210600.1.pHSF family protein
Brast01G240000.1.pHSF family protein
Brast02G050400.1.pHSF family protein
Brast02G100900.1.pHSF family protein
Brast02G191400.1.pHSF family protein
Brast02G304400.1.pHSF family protein
Brast02G340200.1.pHSF family protein
Brast02G340200.2.pHSF family protein
Brast02G388400.1.pHSF family protein
Brast03G129500.1.pHSF family protein
Brast03G129500.2.pHSF family protein
Brast03G298900.1.pHSF family protein
Brast04G184500.1.pHSF family protein
Brast04G195000.1.pHSF family protein
Brast04G242900.1.pHSF family protein
Brast05G145800.1.pHSF family protein
Brast05G146600.1.pHSF family protein
Brast05G188700.1.pHSF family protein
Brast06G035900.1.pHSF family protein
Brast06G196800.1.pHSF family protein
Brast07G142100.1.pHSF family protein
Brast07G142100.2.pHSF family protein
Brast07G147700.1.pHSF family protein
Brast08G050400.1.pHSF family protein
Brast09G175100.1.pHSF family protein
HSF Family Introduction

Heat stress transcription factors (Hsfs) are the major regulators of the plant heat stress (hs) response. Sequencing of the Arabidopsis genome revealed the existence of 21 open-reading frames (ORFs) encoding putative Hsfs assigned to classes A-C. Here we present results of a functional genomics approach to the Arabidopsis Hsf family focused on the analysis of their C-terminal domains (CTDs) harboring conserved modules for their function as transcription factors and their intracellular localization. Using reporter assays in tobacco protoplasts and yeast as well as glutathione-S-transferase (GST) pull-down assays, we demonstrate that short peptide motifs enriched with aromatic and large hydrophobic amino acid (aa) residues embedded in an acidic surrounding (AHA motifs) are essential for transcriptional activity of class A Hsfs. In contrast to this, class B and C Hsfs lack AHA motifs and have no activator function on their own. We also provide evidence for the function of a leucine (Leu)-rich region centered around a conserved QMGΦL motif at the very C-terminus as a nuclear export signal (NES) of class A Hsfs. Sequence comparison indicates that the combination of a C-terminal AHA motif with the consensus sequence FWxxF/L,F/I/L as well as the adjacent NES represents a signature domain for plant class A Hsfs, which allowed to identify more than 60 new Hsfs from the expressed sequence tag (EST) database.

Kotak S, Port M, Ganguli A, Bicker F, von Koskull-Doring P.
Characterization of C-terminal domains of Arabidopsis heat stress transcription factors (Hsfs) and identification of a new signature combination of plant class A Hsfs with AHA and NES motifs essential for activator function and intracellular localization.
Plant J, 2004. 39(1): p. 98-112.
PMID: 15200645