Mapping of domains of heat stress transcription factor OsHsfA6a responsible for its transactivation activity

Copyright © 2018 Elsevier B.V. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant science : an international journal of experimental plant biology. - 1985. - 274(2018) vom: 01. Sept., Seite 80-90
1. Verfasser: Singh, Garima (VerfasserIn)
Weitere Verfasser: Sarkar, Neelam K, Grover, Anil
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2018
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 Plant Proteins
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245 1 0 |a Mapping of domains of heat stress transcription factor OsHsfA6a responsible for its transactivation activity 
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520 |a Copyright © 2018 Elsevier B.V. All rights reserved. 
520 |a 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 
650 4 |a Journal Article 
650 4 |a AHA 
650 4 |a C-terminal activation domain (CTD) 
650 4 |a Heat stress 
650 4 |a Hsp101/ClpB-C 
650 4 |a Nuclear export signal (NES) 
650 4 |a OsHsfA6a 
650 4 |a Rice (Oryza sativa) 
650 4 |a Transactivation activity (TA) 
650 7 |a Heat Shock Transcription Factors  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
700 1 |a Sarkar, Neelam K  |e verfasserin  |4 aut 
700 1 |a Grover, Anil  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Plant science : an international journal of experimental plant biology  |d 1985  |g 274(2018) vom: 01. Sept., Seite 80-90  |w (DE-627)NLM098174193  |x 1873-2259  |7 nnns 
773 1 8 |g volume:274  |g year:2018  |g day:01  |g month:09  |g pages:80-90 
856 4 0 |u http://dx.doi.org/10.1016/j.plantsci.2018.05.010  |3 Volltext 
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