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Brachypodium distachyon strain:Bd1-1, Bd21-3, Bd21, Bd3-1, Bd30-1, BdTR12c, Koz-3

ABSTRACT: Brachypodium distachyon strain:Bd1-1, Bd21-3, Bd21, Bd3-1, Bd30-1, BdTR12c, Koz-3 Transcriptome or Gene expression

PROVIDER: PRJNA253150 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR1427170.fastq.gz	Fastqsanger.gz
	SRR1427171.fastq.gz	Fastqsanger.gz
	SRR1427172.fastq.gz	Fastqsanger.gz
	SRR1427166.fastq.gz	Fastqsanger.gz
	SRR1427167.fastq.gz	Fastqsanger.gz

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Project description:To study the diurnal transcriptome (RNA-seq) expressed by the monocot model plant B. distachyon under submergence stress, we analyzed two different ecotypes (Bd21, submergence sensitive; Bd21-3, submergence tolerant) at 5 different time points (dawn, ZT0; midday, ZT8; dusk, ZT16; middnight ZT20, end of night, ZT24).

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Project description:Bromodomain (BRD) is an epigenetic reader of acetylated lysine. It has emerged as a therapeutic target for cancer and other diseases. Current nonselective BRD inhibitors (BRDis) face several adverse events (i.e. gastrointestinal toxicity and thrombocytopenia), making the development of target covalent inhibitor (TCI) for BD1/2 as a fresh avenue to overcome safety challenges. We report herein a set of activity-based probes (ABPs; P3-P7) based on various lysine-reactive covalent warheads capable of global profiling of ligandable lysine within BRDs in live cells and animals. Chemoproteomic experiments with P7 by utilizing 2-ethynylbenzaldehyde (EBA) identified 16 endogenous BRDs, thus giving a global landscape of ligandable lysines in BRDs. By further introducing EBA and salicylaldehyde into PLX51107 (a non-covalent BRDi), we generated novel irreversible (BDS1-4) and reversible (BDS5-6) lysine-reactive TCIs. Mass spectrometry and X-ray crystallography confirmed the successful covalent engagement between the covalent warhead and lysine near Kac binding site. BDS4 showed 104-fold selectivity for BD1 over BD2 with prolonged anti-cancer effect than non-covalent BRDi. Importantly, BDS4 retained robust activity against fibrosis in cells and animals in comparison to the marginal effect of BD2 inhibitor RVX-208. Our work serves as a useful tool to delineate the distinct function of BD1 and BD2.

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