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Arachis hypogaea

ABSTRACT: Pre-Harvest Aflatoxin Contamination in Groundnut

PROVIDER: PRJNA732524 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14638024_1.fastq.gz	Fastqsanger.gz
	SRR14638024_2.fastq.gz	Fastqsanger.gz
	SRR14638025_1.fastq.gz	Fastqsanger.gz
	SRR14638025_2.fastq.gz	Fastqsanger.gz
	SRR14638026_1.fastq.gz	Fastqsanger.gz

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Profile comparisons of stored mRNA in dry maize seeds from two closely-related geneotypes varying in aflatoxin accumulation

Project description:Aflatoxin contamination occurring after infection by Aspergillus flavus is a major concern in maize production both pre- and post-harvest. A recent gene expression study of imbibed kernels highlighted induced resistance and gene regulation in kernels. In the present study, stored mRNA was profiled using oligo-nucleotide array. This comparison of stored mRNAs would enhance our understanding of the difference between resistant and susceptible lines at the kernel storage phase. To minimize the effect of different genetic backgrounds on the differential genes between resistant and susceptible lines, two closely related inbred lines were used. Of the two lines, Eyl25 is aflatoxin-resistant (R), and Eyl31 is –susceptible (S). These were derived from a cross between two resistant lines, 1368 and GT-MASK:gk, in the IITA and USDA- ARS collaborative breeding project.

2012-07-30 | GSE34434 | GEO

Profile comparisons of stored mRNA in dry maize seeds from two closely-related geneotypes varying in aflatoxin accumulation

2012-07-29 | E-GEOD-34434 | biostudies-arrayexpress

Developmental Analysis of compound leaf development in Arachis hypogaea

Project description:Transcriptomic profiles revealed that the common and unique different expression genes were identified in lateral leaflet and terminal leaflet, using petiole as a control.What's more, transcriptomic analysis was performed to compare the difference of a natural mutant with pentafoliate defects and wild type.

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Role of carbohydrate moieties in peanut (Arachis hypogaea) peroxidases.

Project description:The activities of a cationic (C.PRX) and an anionic peroxidase isolated from peanut (Arachis hypogaea)-cell suspension culture were drastically reduced when they were deglycosylated with glycopeptidase F or oxidized by 10 mM-periodate. In contrast with the controls, the deglycosylated or the oxidized peroxidases were much more susceptible to proteolytic degradation. In radiolabelling experiments with [35S]methionine, the non-glycosylated C.PRX was synthesized in the tunicamycin-treated cultures and secreted into the medium. Examination of the C.PRX polypeptides by SDS/polyacrylamide-gel electrophoresis followed by fluorography showed that the non-glycosylated form had an Mr of approx. 31,000, which is about 78% of that of the glycosylated form. Our results suggest that carbohydrates may not be essential for peroxidase secretion, but that stabilization of the peroxidase molecules and acquisition by these isoenzymes of a catalytically active conformation is linked directly or indirectly to glycosylation.

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