PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Pseudotsuga menziesii
HSF Family
Species TF ID Description
PSME_00001672-RAHSF family protein
PSME_00006388-RAHSF family protein
PSME_00008515-RAHSF family protein
PSME_00009011-RAHSF family protein
PSME_00012433-RAHSF family protein
PSME_00016852-RAHSF family protein
PSME_00020770-RAHSF family protein
PSME_00022202-RAHSF family protein
PSME_00022238-RAHSF family protein
PSME_00029303-RAHSF family protein
PSME_00029305-RAHSF family protein
PSME_00029306-RAHSF family protein
PSME_00029356-RAHSF family protein
PSME_00033358-RAHSF family protein
PSME_00034387-RAHSF family protein
PSME_00034388-RAHSF family protein
PSME_00034737-RAHSF family protein
PSME_00034738-RAHSF family protein
PSME_00037754-RAHSF family protein
PSME_00037755-RAHSF family protein
PSME_00042828-RAHSF family protein
PSME_00049294-RAHSF family protein
PSME_00049940-RAHSF family protein
PSME_00053293-RAHSF family protein
PSME_00053758-RAHSF family protein
PSME_00053883-RAHSF family protein
PSME_00054542-RAHSF family protein
PSME_00055440-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