TY  - JOUR
A1  - Baniwal, Sanjeev Kumar
A1  - Chan, Kwan Yu
A1  - Scharf, Klaus-Dieter
A1  - Nover, Lutz
T1  - Role of heat stress transcription factor HsfA5 as specific repressor of HsfA4
T2  - Journal of biological chemistry
N2  - Unlike other eukaryotes, plants possess a complex family of heat stress transcription factors (Hsfs) with usually more than 20 members. Among them, Hsfs A4 and A5 form a group distinguished from other Hsfs by structural features of their oligomerization domains and by a number of conserved signature sequences. We show that A4 Hsfs are potent activators of heat stress gene expression, whereas A5 Hsfs act as specific repressors of HsfA4 activity. The oligomerization domain of HsfA5 alone is necessary and sufficient to exert this effect. Due to the high specificity of the oligomerization domains, other class A Hsfs are not affected. Pull-down assay and yeast two-hybrid interaction tests demonstrate that the tendency to form HsfA4/A5 heterooligomers is stronger than the formation of homooligomers. The specificity of interaction between Hsfs A4 and A5 was confirmed by bimolecular fluorescence complementation experiments. The major role of the representatives of the HsfA4/A5 group, which are not involved in the conventional heat stress response, may reside in cell type-specific functions connected with the control of cell death triggered by pathogen infection and/or reactive oxygen species.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/76310
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-763108
SN  - 0021-9258
VL  - 282.2007
IS  - 6
SP  - 3605
EP  - 3613
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -