Protein phosphorylation associated with drought priming-enhanced heat tolerance in a temperate grass species

Abstract

Protein phosphorylation is known to play crucial roles in plant tolerance to individual stresses, but how protein phosphorylation is associated with cross-stress tolerance, particularly drought priming-enhanced heat tolerance is largely unknown. The objectives of the present study were to identify phosphorylated proteins and phosphorylation sites that were responsive to drought priming and to determine whether drought priming-enhanced heat tolerance in temperate grass species involves changes in protein phosphorylation. Comparative analysis of phosphoproteomic profiles was performed on leaves of tall fescue (Festuca arundinacea) exposed to heat stress (38/33 °C, day/night) with or without drought priming. A total of 569 differentially regulated phosphoproteins (DRPs) with 1098 phosphorylation sites were identified in response to drought priming or heat stress individually or sequentially. Most DRPs were nuclear-localized and cytosolic proteins. Motif analysis detected [GS], [DSD], and [S..E] as major phosphorylation sites in casein kinase-II and mitogen-activated protein kinases regulated by drought priming and heat stress. Functional annotation and gene ontology analysis demonstrated that DRPs in response to drought priming and in drought-primed plants subsequently exposed to heat stress were mostly enriched in four major biological processes, including RNA splicing, transcription control, stress protection/defense, and stress perception/signaling. These results suggest the involvement of post-translational regulation of the aforementioned biological processes and signaling pathways in drought priming memory and cross-tolerance with heat stress in a temperate grass species.

Common microgeographical selection patterns revealed in four European conifers

“…Remarkably, one study on a tree species, Populus trichocarpa (Evans et al, 2014), found four GO terms (hydrolase activity acting on acid anhydrides, GO:0016817; nucleobase‐containing compound kinase activity, GO:0019205; organic cyclic compound binding, GO:0097159; and heterocyclic compound binding, GO:1901363), out of the 12 reported here, as being associated with adaptive traits (mostly, growth rates and leaf phenology). Organic cyclic compound binding and heterocyclic compound binding were also found in several studies investigating plant responses to abiotic stresses (Alves da Silva et al, 2019; Liu et al, 2017; Safdarian et al, 2019; Zhang et al, 2020; Zhou et al, 2016).…”

“…The GO terms enriched in this study were also enriched in previous plant studies in response to biotic and abiotic variables. Remarkably, one study on a tree species, Populus trichocarpa (Evans et al, 2014) Liu et al, 2017;Safdarian et al, 2019;Zhang et al, 2020;Zhou et al, 2016). putatively under selection is very small.…”

Comprehensive Phosphoproteomic Analysis of Nostoc flagelliforme in Response to Dehydration Provides Insights into Plant ROS Signaling Transduction

“…Although many proteins related to light-harvesting complexes phycobilisome such as cpcA, cpcB, apcA, apcB, and apcF, as well as PsbO, as a component of reaction center in PSII, photosystem II oxygen-evolving enhancer protein1 and DUF2382 domain-containing protein as photosystem reaction center subunit were phosphorylated; while only a few phosphoproteins involved in PSI and PSII show substantial changes for phosphorylation levels (Figure ), which indicates the integrity of PSI and PSII photosynthetic system could allow very quick response to rehydration for N. flagelliforme. Several photosynthetic proteins are reported to be involved in various abiotic stress, including water shortage stress as reported by Zhang et al, however, the phosphoproteins, identified in our study are involved in the response to water stress, suggesting the protein degradation or activity could play important role in this response, explained by Parry and his co-workers, this could be due to regulation of some upstream protein kinase as suggested by Chen et al, Therefore, in this study, we confirmed that some proteins involved in the photosynthetic pathway can be phosphorylated, and the modification of phosphorylation is important for plant adaption to abiotic stress.…”

Regulatory Networks of lncRNAs, miRNAs, and mRNAs in Response to Heat Stress in Wheat (Triticum Aestivum L.): An Integrated Analysis

“…The GO term categorized for the biological process GO:0055114 was prominently found under 0 DAT and 1 DAT conditions, confirming the oxidation-reduction process which is central to both genetic and epigenetic control of plant responses to heat stress [ 69 , 70 ]. The other noticeable GO terms under the biological process were GO:0006355, GO:0016310, and GO:0006468, associated with the regulation of transcription [ 71 , 72 ], phosphorylation, and protein phosphorylation [ 73 , 74 ], which showed regulating heat stress in plants.…”