ATP and Mg2+ promote the reversible oligomerization and aggregation of chloroplast 2-Cys peroxiredoxin

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2-Cys peroxiredoxins (2-Cys Prxs) are ubiquitous peroxidases with important roles in cellular antioxidant defense and hydrogen peroxide-mediated signaling. Post-translational modifications of conserved cysteines cause the transition from low to high molecular weight oligomers, triggering the functio...

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Detalles Bibliográficos
Autores principales: Aran, M., Ferrero, D., Wolosiuk, A., Mora-García, S., Wolosiuk, R.A.
Formato: Artículo publishedVersion
Lenguaje:Inglés
Publicado: 2011
Materias:
2 ,2 ,2-trifluoroethanol
Antioxidant defense
Chaperone activity
Conserved residues
Cosolvents
Cysteine residues
Decamers
Functional changes
Helical conformation
Higher order
In-line
Low-to-high
Molecular chaperones
Native conformation
Non-covalent interaction
Peroxiredoxins
Post-translational modifications
Quaternary structure
Redox transformations
Self-polymerization
Amino acids
Chlorophyll
Conformations
Dichroism
Ethanol
Hydrogen peroxide
Oligomerization
Polymerization
Spheres
Transmission electron microscopy
Oligomers
2 cysteine peroxiredoxin
adenosine triphosphate
arginine
cysteine
magnesium ion
peroxiredoxin
trifluoroethanol
unclassified drug
magnesium
recombinant protein
vegetable protein
alpha helix
article
beta sheet
cell energy
chloroplast
circular dichroism
controlled study
enzyme activity
enzyme regulation
molecular interaction
molecular weight
nonhuman
oligomerization
oxidation reduction reaction
particle size
photochemistry
priority journal
protein aggregation
protein analysis
protein conformation
protein function
protein polymerization
protein processing
protein quaternary structure
rapeseed
surface plasmon resonance
transmission electron microscopy
chemistry
enzymology
genetics
metabolism
protein multimerization
protein secondary structure
Adenosine Triphosphate
Chloroplasts
Circular Dichroism
Magnesium
Plant Proteins
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Secondary
Recombinant Proteins
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00219258_v286_n26_p23441_Aran
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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