Identification and expression profiling of GAPDH family genes involved in response to Sclerotinia sclerotiorum infection and phytohormones in Brassica napus
Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a crucial enzyme in glycolysis, an essential metabolic pathway for carbohydrate metabolism across all living organisms. Recent research indicates that phosphorylating GAPDH exhibits various moonlighting functions, contributing to plant growth and d...
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Veröffentlicht in: | Frontiers in plant science 2024-04, Vol.15, p.1360024-1360024 |
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Sprache: | eng |
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Zusammenfassung: | Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a crucial enzyme in glycolysis, an essential metabolic pathway for carbohydrate metabolism across all living organisms. Recent research indicates that phosphorylating GAPDH exhibits various moonlighting functions, contributing to plant growth and development, autophagy, drought tolerance, salt tolerance, and bacterial/viral diseases resistance. However, in rapeseed (
), the role of GAPDHs in plant immune responses to fungal pathogens remains unexplored. In this study, 28 genes encoding GAPDH proteins were revealed in
and classified into three distinct subclasses based on their protein structural and phylogenetic relationships. Whole-genome duplication plays a major role in the evolution of
. Synteny analyses revealed orthologous relationships, identifying 23, 26, and 26
genes with counterparts in
,
, and
, respectively. The promoter regions of 12
uncovered a spectrum of responsive elements to biotic and abiotic stresses, indicating their crucial role in plant stress resistance. Transcriptome analysis characterized the expression profiles of different
genes during
infection and hormonal treatment. Notably,
,
,
, and
exhibited sensitivity to
infection, oxalic acid, hormone signals. Intriguingly, under standard physiological conditions,
,
, and
are primarily localized in the cytoplasm and plasma membrane, with
also detectable in the nucleus. Furthermore, the nuclear translocation of
was observed under H
O
treatment and
infection. These findings might provide a theoretical foundation for elucidating the functions of phosphorylating GAPDH. |
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ISSN: | 1664-462X 1664-462X |
DOI: | 10.3389/fpls.2024.1360024 |