Mapping of domains of heat stress transcription factor OsHsfA6a responsible for its transactivation activity
Copyright © 2018 Elsevier B.V. All rights reserved.
| Veröffentlicht in: | Plant science : an international journal of experimental plant biology. - 1985. - 274(2018) vom: 01. Sept., Seite 80-90 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2018
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| Zugriff auf das übergeordnete Werk: | Plant science : an international journal of experimental plant biology |
| Schlagworte: | Journal Article AHA C-terminal activation domain (CTD) Heat stress Hsp101/ClpB-C Nuclear export signal (NES) OsHsfA6a Rice (Oryza sativa) Transactivation activity (TA) Heat Shock Transcription Factors |
| Zusammenfassung: | Copyright © 2018 Elsevier B.V. All rights reserved. Elevated temperatures affect the growth and reproduction of crop plants and thus have become concern worldwide. Hsp101/ClpB protein is a major molecular chaperone, performing dis-aggregation of protein aggregates formed during heat stress. In rice, OsHsfA6a binds to the promoter of OsHsp101/ClpB-C and regulates its expression. In this study, analysis of C-terminal domains of ClassA OsHsfs revealed the presence of aromatic, hydrophobic, acidic (AHA) and nuclear export signal (NES) motifs in all the members. Using deletion constructs, we show that the activation potential of OsHsfA6a is confined in the C-terminal activation domain comprising of AHA and NES sequences. The results obtained in yeast were complemented with transient expression of reporter in protoplast (TERP) based assay. Detailed analysis of OsHsfA6a splice variants shows the presence of one full version and a DBD truncated smaller version whose existence needs experimental evidences. Phylogeny analysis revealed that OsHsfA6a has diverged from A6a/A6b forms of Arabidopsis and tomato and has no expressologs. OsHsfA6a in-silico network was enriched in MAP kinases along with Hsp70 and Hsp90 proteins. Thus, it appears that regulation of OsClpB-C by HsfA6a is unique in rice and activation potential of OsHsfA6a resides in the single AHA motif located in the C-terminal domain |
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| Beschreibung: | Date Completed 09.10.2018 Date Revised 07.12.2022 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1873-2259 |
| DOI: | 10.1016/j.plantsci.2018.05.010 |