Meleagris gallopovo
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA810919 | ENA |
REPOSITORIES: ENA
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2015-03-11 | GSE66704 | GEO
Project description:Multigenicity is commonly found in fungal enzyme systems, with the purpose of functional compensation upon deficiency of one of its members or leading to enzyme isoforms with new functionalities through gene diversification. Three genes of the flavin-dependent glucose-methanol-choline (GMC) oxidoreductase pyranose dehydrogenase (AmPDH) were previously identified in the litter-degrading fungus Agaricus (Leucoagaricus) meleagris, of which only AmPDH1 was successfully expressed and characterized. The aim of this work was to study the biophysical and biochemical properties of AmPDH2 and AmPDH3 and compare them with those of AmPDH1. AmPDH1, AmPDH2 and AmPDH3 showed negligible oxygen reactivity and possess a covalently tethered FAD cofactor. All three isoforms can oxidise a range of different monosaccarides and oligosaccharides including glucose, mannose, galactose and xylose, which are the main constituent sugars of cellulose and hemicelluloses, and judging from the apparent steady-state kinetics determined for these sugars, the three isoforms do not show significant differences pertaining to their reaction with sugar substrates. They oxidize glucose both at C2 and C3 and upon prolonged reaction C2 and C3 double-oxidized glucose is obtained, confirming that the A. meleagris genes pdh2 (AY753308.1) and pdh3 (DQ117577.1) indeed encode CAZy class AA3_2 pyranose dehydrogenases. While reactivity with electron donor substrates was comparable for the three AmPDH isoforms, their kinetic properties differed significantly for the model electron acceptor substrates tested, a radical (the 2,2'-azino-bis[3-ethylbenzothiazoline-6-sulphonic acid] cation radical), a quinone (benzoquinone) and a complexed iron ion (the ferricenium ion). Thus, a possible explanation for this PDH multiplicity in A. meleagris could be that different isoforms react preferentially with structurally different electron acceptors in vivo.
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Project description:The objective of this study was to determine differential gene expression of turkey breast muscle regarding development of PSE meat defect. Genetically unimproved, random-bred (RBC2) turkeys representing turkeys from 1966, which are smaller and grow slower than modern turkeys, were raised at the Michigan State University (MSU) Poultry farm and harvested at 22 week of age. Breast meat was collected and snap frozen in liquid nitrogen. Percent marinade uptake at 24h post-slaughter of each sample was determined. The highest (n=6) and the lowest (n=6) marinade uptake were classified as normal and PSE, respectively. Differentially expressed genes between normal and PSE was identified using TSMLO microarray and confirmed by qRT-PCR. Forty-one oligos were differentially expressed (false discovery rate, FDR<0.1). Candidate genes and pathways associated with development of PSE in turkey were suggested for further experiment to gain greater comprehension about this meat quality defect.
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