Maize HEAT UP-REGULATED GENE 1 plays vital roles in heat stress tolerance

© The Author(s) 2022. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 73(2022), 18 vom: 18. Okt., Seite 6417-6433
1. Verfasser: Xie, Chen (VerfasserIn)
Weitere Verfasser: Yang, Liu, Jia, Guixian, Yan, Kang, Zhang, Shizhong, Yang, Guodong, Wu, Changai, Gai, Yingping, Zheng, Chengchao, Huang, Jinguang
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2022
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Chaperone ZmHUG1 ZmPRA1.C1 heat stress maize stress Protein Aggregates Molecular Chaperones
Beschreibung
Zusammenfassung:© The Author(s) 2022. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
Increasing temperature is one of the major threats to maize growth and yield globally. Under heat stress conditions, intracellular protein homeostasis is seriously disturbed, leading to accumulation of abnormally folded proteins, especially in the endoplasmic reticulum (ER). Molecular chaperones are vital players in the renaturation process and in preventing protein aggregation. However, heat stress tolerance-associated chaperones are not well documented in maize. Here, we characterized the biological roles of HEAT UP-REGULATED GENE 1 (ZmHUG1) in maize. ZmHUG1 encodes a heat-inducible holdase-type molecular chaperone localized in the ER. Knockout mutant of ZmHUG1 exhibited remarkably enhanced sensitivity to heat stress. Accordingly, the zmhug1 mutant showed severe ER stress under high temperature. MAIZE PRENYLATED RAB ACCEPTOR 1.C1 (ZmPRA1.C1) was identified as a client of ZmHUG1, and heat-induced aggregation of ZmPRA1.C1 was accelerated in the zmhug1 mutant. Furthermore, the expression of ZmHUG1 was rapidly transactivated by ER stress sensor BASIC LEUCINE ZIPPER DOMAIN 60 (bZIP60) when heat stress occurred. This study reveals a ZmHUG1-based thermo-protective mechanism in maize
Beschreibung:Date Completed 20.10.2022
Date Revised 21.10.2022
published: Print
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erac262