Genome-wide identification of sweet potato U-Box E3 ubiquitin ligases and roles of IbPUB52 in negative regulation of drought stress.

Physiol Plant

Key Laboratory of National Forestry and Grassland Administration on Plant Conservation and Utilization in Southern China & Guangdong Provincial Key Laboratory of Applied Botany, South China Botanical Garden, Chinese Academy of Sciences, Guangzhou, China.

Published: October 2024

The plant U-box (PUB) proteins, a family of ubiquitin ligases (E3) enzymes, are pivotal in orchestrating many biological processes and facilitating plant responses to environmental stressors. Despite their critical roles, exploring the PUB gene family's characteristics and functional diversity in sweet potato (Ipomoea batatas (L.) Lam.) has been notably limited. There were 81 IbPUB genes identified within the sweet potato genome, and they were categorized into eight distinct groups based on domain architecture, revealing a non-uniform distribution across the 15 chromosomes of I. batatas. The investigation of cis-acting elements has shed light on the potential of PUBs to participate in a wide array of biological processes, particularly emphasizing their role in mediating responses to abiotic stresses. Transcriptome profiles revealed that IbPUB genes displayed a wide range of expression levels among different tissues and were regulated by salt or drought stress. IbPUB52 has emerged as a gene of significant interest due to its induction by salt and drought stresses. Localization studies have confirmed the presence of IbPUB52 in both the nucleus and the cytoplasm, and its ubiquitination activity has been validated through rigorous in vitro and in vivo assays. Intriguingly, the heterogeneous expression of IbPUB52 in Arabidopsis resulted in decreased drought tolerance. The virus-induced gene silencing (VIGS) of IbPUB52 in sweet potatoes led to enhanced resistance to drought. This evidence suggests that IbPUB52 negatively regulates the drought tolerance of plants. The findings of this study are instrumental in advancing our comprehension of the functional dynamics of PUB E3 ubiquitin ligases in sweet potatoes.

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http://dx.doi.org/10.1111/ppl.14568DOI Listing

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