Plant Transcription Factor Database
Previous version: v3.0
Juglans regia
HSF Family
Species TF ID Description
WALNUT_00000780-RAHSF family protein
WALNUT_00000781-RAHSF family protein
WALNUT_00000909-RAHSF family protein
WALNUT_00002234-RAHSF family protein
WALNUT_00004368-RAHSF family protein
WALNUT_00005965-RAHSF family protein
WALNUT_00007546-RAHSF family protein
WALNUT_00008359-RAHSF family protein
WALNUT_00009520-RAHSF family protein
WALNUT_00009584-RAHSF family protein
WALNUT_00011112-RAHSF family protein
WALNUT_00011576-RAHSF family protein
WALNUT_00015075-RAHSF family protein
WALNUT_00016513-RAHSF family protein
WALNUT_00016524-RAHSF family protein
WALNUT_00016643-RAHSF family protein
WALNUT_00017122-RAHSF family protein
WALNUT_00017448-RAHSF family protein
WALNUT_00017547-RAHSF family protein
WALNUT_00017615-RAHSF family protein
WALNUT_00019208-RAHSF family protein
WALNUT_00019696-RAHSF family protein
WALNUT_00020872-RAHSF family protein
WALNUT_00023778-RAHSF family protein
WALNUT_00023834-RAHSF family protein
WALNUT_00024234-RAHSF family protein
WALNUT_00026458-RAHSF family protein
WALNUT_00026813-RAHSF family protein
WALNUT_00028022-RAHSF family protein
WALNUT_00028244-RAHSF family protein
WALNUT_00029061-RAHSF 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