期刊
PLANT CELL AND ENVIRONMENT
卷 41, 期 8, 页码 1852-1869出版社
WILEY
DOI: 10.1111/pce.13326
关键词
cochaperone; HSP70-HSP90 organizing protein; HSP90; LAT; plants; QC; quality control
资金
- FP7 Ideas: European Research Council [260468]
- Instituto Nacional de Investigacion Agraria y Agroalimentaria (INIA) [RTA2013-00027-00-00]
- Comunidad de Madrid [S2013-ABI2748]
- European Research Council (ERC) [260468] Funding Source: European Research Council (ERC)
HSP70-HSP90 organizing protein (HOP) is a family of cytosolic cochaperones whose molecular role in thermotolerance is quite unknown in eukaryotes and unexplored in plants. In this article, we describe that the three members of the AtHOP family display a different induction pattern under heat, being HOP3 highly regulated during the challenge and the attenuation period. Despite HOP3 is the most heat-regulated member, the analysis of the hop1 hop2 hop3 triple mutant demonstrates that the three HOP proteins act redundantly to promote long-term acquired thermotolerance in Arabidopsis. HOPs interact strongly with HSP90 and part of the bulk of HOPs shuttles from the cytoplasm to the nuclei and to cytoplasmic foci during the challenge. RNAseq analyses demonstrate that, although the expression of the Hsf targets is not generally affected, the transcriptional response to heat is drastically altered during the acclimation period in the hop1 hop2 hop3 triple mutant. This mutant also displays an unusual high accumulation of insoluble and ubiquitinated proteins under heat, which highlights the additional role of HOP in protein quality control. These data reveal that HOP family is involved in different aspects of the response to heat, affecting the plant capacity to acclimate to high temperatures for long periods.
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