Characterization of a globin-coupled oxygen sensor with a gene-regulating function

Autor: Evi Vinck, Paolo Ascenzi, Alessandro Bolli, Roy E. Weber, Sylvia Dewilde, Angela Fago, Liesbet Thijs, Sabine Van Doorslaer, David Hoogewijs, Massimiliano Coletta, Maqsudul Alam, Xuehua Wan, Florin Trandafir, L. Moens
Přispěvatelé: Thijs, L, Vinck, E, Bolli, A, Trandafir, F, Wan, X, Hoogewijs, D, Coletta, M, Fago, A, Weber, Re, VAN DOORSLAER, S, Ascenzi, Paolo, Alam, M, Moens, L, Dewilde, S.
Jazyk: angličtina
Rok vydání: 2007
Předmět:
ferrous ion
molecular cloning
Conformational change
Time Factors
Bacteria
Carbonylation
Genes
Isotherms
Ligands
Proteins
Archaea
Globin coupled sensors (GCS)
Oxygen sensors
bacterial protein
carbon monoxide
globin
heme
iron
myoglobin
protein AvGReg
protein AvGReg178
Archaebacterium
article
Azotobacter vinelandii
bacterium
binding affinity
carbonylation
conformational transition
detoxification
gene control
nonhuman
nucleotide sequence
oxygen dissociation curve
oxygen sensing
priority journal
protein domain
protein expression
protein function
protein purification
signal transduction
Amino Acid Sequence
Bacterial Proteins
Escherichia coli
Gene Expression Regulation
Bacterial

Heme
Hemeproteins
Histidine
Iron
Kinetics
Models
Biological

Molecular Sequence Data
Nitric Oxide
Oxygen
Protein Structure
Tertiary

Sequence Homology
Amino Acid

Spectrum Analysis
Raman

Sequence Homology
Biochemistry
chemistry.chemical_compound
Models
Raman
biology
Bacterial
Amino Acid
Myoglobin
medicine.drug
Protein Structure
Stereochemistry
Ferrous
TheoryofComputation_ANALYSISOFALGORITHMSANDPROBLEMCOMPLEXITY
medicine
Globin
Settore BIO/10
Molecular Biology
Spectrum Analysis
Cell Biology
biology.organism_classification
Biological
chemistry
Gene Expression Regulation
Ferric
Tertiary
Zdroj: Thijs, L, Vinck, E, Bolli, A, Trandafir, F, Wan, X, Hoogewijs, D, Coletta, M, Fago, A, Weber, R E, Doorslaer, S V, Ascenzi, P, Alam, M, Moens, L & Dewilde, S 2007, ' Characterization of a globin-coupled oxygen sensor with a gene-regulating function ', Journal of Biological Chemistry, vol. 282, no. 52, pp. 37325-37340 . https://doi.org/10.1074/jbc.M705541200
Journal of biological chemistry
ISSN: 0021-9258
DOI: 10.1074/jbc.M705541200
Popis: Globin-coupled sensors (GCSs) are multiple-domain transducers, consisting of a regulatory globin-like heme-binding domain and a linked transducer domain(s). GCSs have been described in both Archaea and bacteria. They are generally assumed to bind O2 (and perhaps other gaseous ligands) and to transmit a conformational change signal through the transducer domain in response to fluctuating O2 levels. In this study, the heme-binding domain, AvGReg178, and the full protein, AvGReg of the Azotobacter vinelandii GCS, were cloned, expressed, and purified. After purification, the heme iron of AvGReg178 was found to bind O2. This form was stable over many hours. In contrast, the predominant presence of a bis-histidine coordinate heme in ferric AvGReg was revealed. Differences in the heme pocket structure were also observed for the deoxygenated ferrous state of these proteins. The spectra showed that the deoxygenated ferrous derivatives of AvGReg178 and AvGReg are characterized by a penta-coordinate and hexa-coordinate heme iron, respectively. O2 binding isotherms indicate that AvGReg178 and AvGReg show a high affinity for O2 with P50 values at 20 °C of 0.04 and 0.15 torr, respectively. Kinetics of CO binding indicate that AvGReg178 carbonylation conforms to a monophasic process, comparable with that of myoglobin, whereas AvGReg carbonylation conforms to a three-phasic reaction, as observed for several proteins with bis-histidine heme iron coordination. Besides sensing ligands, in vitro data suggest that AvGReg(178) may have a role in O2-mediated NO-detoxification, yielding metAvGReg(178) and nitrate.
Databáze: OpenAIRE