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ABSTRACT: BSA-Seq for a yellow-to-lethal mutant

PROVIDER: PRJNA1061757 | ENA |

REPOSITORIES: ENA

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Dataset's files

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			Action	DRS
	SRR27446267_1.fastq.gz	Fastqsanger.gz
	SRR27446267_2.fastq.gz	Fastqsanger.gz
	SRR27446268_1.fastq.gz	Fastqsanger.gz
	SRR27446268_2.fastq.gz	Fastqsanger.gz

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Similar Datasets

Revealing the key role of the folate synthesis regulatory gene DHNA in tobacco leaf yellowing based on BSA-seq, RNA-seq, and proteomic sequencing

Project description:The degree of yellowing in tobacco leaves is an important indicator for determining the maturity and harvesting time of tobacco leaves. Reduction in chlorophyll is of utility for promoting the concentrated maturation of tobacco leaves and achieving mechanised harvesting and mining, and utilising tobacco yellow leaf regulatory genes is of great significance for the selection and breeding of tobacco varieties suitable for mechanised harvesting and the resolution of the molecular mechanisms controlling leaf colouration. In this study, the phenotypes of the yellow-leaf K326 and K326 varieties were analysed, and it was observed that the yellow-leaf K326 variety exhibited a distinct yellow leaf phenotype with a significant reduction in chlorophyll content. Subsequently, using a combination of BSA-seq, transcriptomic sequencing (RNA-seq), and proteomic sequencing approaches, we identified the candidate gene Nitab4.5_0008674g0010 that encodes dihydroneopterin aldolase as a factor associated with tobacco leaf yellowing. Finally, by measuring the folate content in K326 and Huangye K326, the folate content in Huangye K326 was observed to be significantly lower than that in K326, thus indicating that folate synthesis plays a crucial role in phenotypic changes in tobacco yellow leaves. This study is the first to use BSA-seq combined with RNA-seq and proteomic sequencing to identify candidate genes in tobacco yellow leaves. The results provide a theoretical basis for the analysis of the mechanism of tobacco yellow leaf mutations.

2024-10-23 | GSE270039 | GEO

The histone chaperone HIR establishes chromatin states controling nitrogen assimilation and virulence in Candida albicans [ATAC-seq]

Project description:ATAC-seq analysis of wild type C. albicans and a HIR1 gene deletion mutant during nutrient rich growth (YPD) and upon the shift to nitrogen starvation in yeast carbon base medium supplemented with BSA (YCB-BSA medium).

2020-12-31 | GSE157568 | GEO

Project description:BSA-seq of cucumber Virescent mutant

| PRJNA844414 | ENA

Project description:BSA-Seq and RNA-Seq of Morex and ygl8 mutant

| PRJNA1027084 | ENA

Proteome sequencing of tobacco yellow leaf mutants

Project description:Subsequently, using a combination of BSA-seq, transcriptomic sequencing (RNA-seq), and proteomic sequencing approaches, we identified the candidate gene Nitab4.5_0008674g0010 that encodes dihydroneopterin aldolase as a factor associated with tobacco leaf yellowing.

2024-06-15 | PXD053162 |

The histone chaperone HIR establishes chromatin states controling nitrogen assimilation and virulence in Candida albicans [RNA-seq]

Project description:Transcriptomic analysis of wild type C. albicans and a HIR1 gene deletion mutant during nutrient rich growth (YPD) and upon the shift to nitrogen starvation in yeast carbon base medium supplemented with BSA (YCB-BSA medium).

2020-12-31 | GSE157411 | GEO

Mus musculus

Project description:Pioglitazone treatment of Lethal Yellow mice

| PRJNA102117 | ENA

Project description:BSA-seq

| PRJNA1132379 | ENA

Project description:BSA-seq

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iPRG 2009: Differential proteomics in Orbitrap E. coli lysates

Project description:The files in directory were generated as part of the ABRF iPRG 2009 Study. The sample is E. coli lysate. The five "red" RPLC runs lack the "green" set of proteins. The five "yellow" runs lack the "blue" set of proteins. Both red and yellow runs contain a spike of BSA to enable quantitative comparison among runs. Proteins were reduced and alkylated by DTT and iodoacetamide, respectively, and separated in a 1D gel. The proteins were trypsinized, and the peptides were added to the in-solution digest of BSA. In a collaboration between the Ayers Institute and Mass Spectrometry Research Center at Vanderbilt University Medical Center, the red and yellow samples were each separated five times in an RPLC/MS/MS experiment lasting 184 minutes (of which the shallow gradient lasted two hours ). The instrument collecting data was a Thermo LTQ-XL Orbitrap. Eight centroided tandem mass spectra were collected following each profile MS scan. Collection of these data was supported by U24 CA126479.

2014-01-28 | MSV000078539 | MassIVE

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