Genome-wide analysis on characterization of LEA gene family in responses to dehydration stress in recalcitrant Panax notoginseng seeds

Author:

Jia Jin-Shan1,Ge Na1,Wang Qing-Yan1,Zhao Li-Ting1,Chen Cui1,Chen Jun-Wen1

Affiliation:

1. Yunnan Agricultural University

Abstract

Abstract Background Late embryogenesis abundant (LEA) proteins play an important role in dehydration process of seed maturation. The seeds of Panax notoginseng (Burkill) F. H. Chen are typically characterized with the recalcitrance and are highly sensitive to dehydration. However, it is not very well known about the role of LEA proteins in response to dehydration stress in P. notoginseng seeds. A genome-wide analysis would be performed in the LEA gene family of recalcitrant P. notoginseng seeds to learn more about the function of LEA proteins in response to dehydration stress. Results In this study, 61 LEA genes were identified from the P. notoginseng genome, and they were renamed as PnoLEA. The PnoLEA genes were classified into seven subfamilies based on the phylogenetic relationships, gene structure and conserved domains. The PnoLEA genes family showed relatively few introns and was highly conserved. Unexpectedly, the LEA_6 subfamily were not found, and the LEA_2 subfamily contained 46 (75.4%) members. Within 19 pairs of fragment duplication events, among them 17 pairs were LEA_2 subfamily. The Ka/Ks ratios are between 0.06 and 0.58 in all the homologous genes pairs, indicating that these homologous genes have experienced a purifying selection. In addition, the expression of the PnoLEA genes was obviously induced under dehydration stress, but the germination rate of P. notoginseng seeds decreased as the dehydration time prolonged. Conclusions We found that the lack of the LEA_6 subfamily, the expansion of the LEA_2 subfamily and low transcriptional levels of most PnoLEA genes might be implicated in the recalcitrant formation of P. notoginseng seeds. LEA proteins are essential in the response to dehydration stress in recalcitrant seeds, but the protective effect of LEA protein is not efficient. These results could improve our understanding of the function of LEA proteins in the response of dehydration stress and their contributions to the formation of seed recalcitrance.

Publisher

Research Square Platform LLC

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