| Literature DB >> 29223066 |
Liang Yang1, Lintao Wu2, Wei Chang3, Zhi Li3, Mingjun Miao3, Yuejian Li3, Junpin Yang4, Zhibin Liu5, Jun Tan6.
Abstract
Ubiquitin-mediated protein degradation plays a crucial role in enabling plants to effectively and efficiently cope with environmental stresses. The E3 ligases have emerged as a central component of the ubiquitination pathway and modulate plant response to abiotic stresses. However, few such studies have been reported in maize. In this study, a C3HC4-type RING finger E3 ligase in maize, ZmAIRP4 (Zea mays Abscisic acid [ABA]-Insensitive RING Protein 4), which is an ortholog of AtAIRP4, was isolated by reverse transcription polymerase chain reaction with specific primers, and its functions in tolerance to drought stress were described. ZmAIRP4 was upregulated by ABA, polyethylene glycol and sodium chloride. In vitro ubiquitination assays and subcellular localization indicated that ZmAIRP4 was an active E3 ligase predominantly localized in the cytoplasm and nucleus. Compared to wild type, ZmAIRP4-overexpressing Arabidopsis plants were hypersensitive to ABA during early seedling development, and showed enhanced drought tolerance. Moreover, the transcript levels of several drought-related downstream genes in transgenic plants were dramatically increased compared with wild type plants. Our results suggested that E3 ligase ZmAIRP4 is a positive regulator in the drought tolerance response pathway.Entities:
Keywords: Drought tolerance; RING E3 ubiquitin ligase; Transgenic Arabidopsis; Zea mays L.
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Year: 2017 PMID: 29223066 DOI: 10.1016/j.plaphy.2017.11.017
Source DB: PubMed Journal: Plant Physiol Biochem ISSN: 0981-9428 Impact factor: 4.270