Aly: a possible E2F interacting protein

Comunicaciones a congreso

Label-free quantification based on data independent acquisition mass spectrometry

Comunicaciones a congreso

Differential protein expression analysis of activated E2F2-/-T lymphocytes by means of label-free quantification method

Comunicaciones a congreso

Validación de la técnica de análisis masivo ("shotgun") con péptidos no marcados para el estudio del proteoma de Botrytis cinerea

Comunicaciones a congreso

Análisis del efecto de la sobreexpresión o silenciamiento de ALY mediante Proteómica diferencial

Comunicaciones a congreso

Gel-free/label-free analysis to study the proteome of botrytis cinerea

Comunicaciones a congreso

The intrinsically disordered distal face of nucleoplasmin recognizes distinct oligomerization states of histones

The role of Nucleoplasmin (NP) as a H2A-H2B histone chaperone has been extensively characterized. To understand its putative interaction with other histone ligands, we have characterized its ability to bind H3-H4 and histone octamers. We find that the chaperone forms distinct complexes with histones, which differ in the number of molecules that build the assembly and in their spatial distribution. When complexed with H3-H4 tetramers or histone octamers, two NP pentamers form an ellipsoidal particle with the histones located at the center of the assembly, in stark contrast with the NP/H2A-H2B complex that contains up to five histone dimers bound to one chaperone pentamer. This particular assembly relies on the ability of H3-H4 to form tetramers either in solution or as part of the octamer, and it is not observed when a variant of H3 (H3C110E), unable to form stable tetramers, is used instead of the wild-type protein. Our data also suggest that the distal face of the chaperone is involved in the interaction with distinct types of histones, as supported by electron microscopy analysis of the different NP/histone complexes. The use of the same structural region to accommodate all type of histones could favor histone exchange and nucleosome dynamics

Causes and management of nutritional rickets among paediatric age group in Rajasthan: a randomised control trial

Background: Rickets disease frequently caused by insufficient of vitamin D. Nevertheless, subsequent researchers have attributed it to a calcium insufficiency throughout the eating plan. There is very little data on the relative efficacy of calcium, vitamin D, or both in the treatment of rickets. The goal of this study was to see if calcium, vitamin D, or a combination of the two may help young infants with nutritional rickets.Methods: 100 patients of nutritional rickets aged 6 months to 5 years were randomly assigned to receive vitamin D (6,00,000 IU single intramuscular injection), calcium (75 mg/kg/day elemental calcium orally) or a combination. All of the participants' demographics, nutritional status, dietary calcium, and phytate consumption were evaluated.Results: More than 80 percent of the patients in the study had 25OHD levels below 20 ng/ml. Rickets was discovered as an afterthought throughout the remaining 60. Lower respiratory illness (40), upper respiratory tract illness (10) and acute gastroenteritis have been the presenting conditions.Conclusions: Children experiencing rickets exhibited low vitamin D levels in their blood as well as a low calcium intake from their nutrition. When compared to either vitamin D or calcium alone, the combination showed the best therapeutic effect.

Cytosolic Fe-S cluster protein maturation and iron regulation are independent of the mitochondrial Erv1/Mia40 import system

The sulfhydryl oxidase Erv1 partners with the oxidoreductase Mia40 to import cysteine-rich proteins in the mitochondrial intermembrane space. In Saccharomyces cerevisiae, Erv1 has also been implicated in cytosolic Fe-S protein maturation and iron regulation. To investigate the connection between Erv1/Mia40-dependent mitochondrial protein import and cytosolic Fe-S cluster assembly, we measured Mia40 oxidation and Fe-S enzyme activities in several erv1 and mia40 mutants. Although all the erv1 and mia40 mutants exhibited defects in Mia40 oxidation, only one erv1 mutant strain (erv1-1) had significantly decreased activities of cytosolic Fe-S enzymes. Further analysis of erv1-1 revealed that it had strongly decreased glutathione (GSH) levels, caused by an additional mutation in the gene encoding the glutathione biosynthesis enzyme glutamate cysteine ligase (GSH1). To address whether Erv1 or Mia40 plays a role in iron regulation, we measured iron-dependent expression of Aft1/2-regulated genes and mitochondrial iron accumulation in erv1 and mia40 strains. The only strain to exhibit iron misregulation is the GSH-deficient erv1-1 strain, which is rescued with addition of GSH. Together, these results confirm that GSH is critical for cytosolic Fe-S protein biogenesis and iron regulation, whereas ruling out significant roles for Erv1 or Mia40 in these pathways