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Chemiosmotic H+ cycling across the plasma membrane of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
Transitory H+ ejection from Sulfolobus acidocaldarius cells induced by oxygen pulses, and anaerobic H+ backflow were investigated. Aerobic proton extrusion is inhibited by protonophores, by nigericin
Variable Oligomerization Modes in Coronavirus Non-structural Protein 9
It is proposed that both forms of the Nsp9 dimer are biologically relevant; the occurrence of the disulfide-bonded form may be correlated with oxidative stress induced in the host cell by the viral infection.
Archaeal complex II: 'classical' and 'non-classical' succinate:quinone reductases with unusual features.
A phylogenetic analysis is presented suggesting a co-evolution of the flavoprotein-binding subunit A and subunit B containing the three iron-sulfur clusters, and a novel class of SQRs is discussed in comparison to the so-called 'classical' complexes.
Domain structure, GTP-hydrolyzing activity and 7S RNA binding of Acidianus ambivalens ffh-homologous protein suggest an SRP-like complex in archaea.
Comparative sequence analysis reveals the presence of typical signal sequences in plasma membrane as well as extracellular proteins of hyperthermophilic crenarchaea which strongly supposes recognition events by an Ffh containing SRP-like particle in these organisms.
Has Sulfolobus an Archaic Respiratory System? Structure, Function and Genes of its Components
A tentative scheme of the electron transport system from Sulfolobus is proposed and sequence comparisons are discussed with regard to the question, as to whether it resembles a primitive “archaic” precursor form of more complex “modern” respiratory systems, or whether it evolved by aquisition and adaptation of “foreign” genes.
Purification and characterisation of an archaebacterial succinate dehydrogenase complex from the plasma membrane of the thermoacidophile Sulfolobus acidocaldarius.
A succinate dehydrogenase complex was isolated in a three-step purification from plasma membranes of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius, and the succinate--phenazine methosulfate-(1,4-dichloroindophenol) oxidoreductase of the isolated complex was strongly inhibited by tetrachlorobenzoquinone.
A succinate dehydrogenase with novel structure and properties from the hyperthermophilic archaeon Sulfolobus acidocaldarius: genetic and biophysical characterization
Electron paramagnetic resonance (EPR) spectroscopic studies of the purified enzyme as well as of membranes revealed the presence of typical S1 [2Fe2S] and S2 [4Fe4S] clusters, congruent with the deduced amino acid sequences.
Purification, cloning, and sequencing of archaebacterial pyrophosphatase from the extreme thermoacidophile Sulfolobus acidocaldarius.
The highest similarity is found with the enzyme from the phylogenetically extremely distant eubacterium E. coli, but immunological cross-reactivity is absent and similarity to the only known other archaebacterial PPase is much weaker.
The crystal structure of the conserved GTPase of SRP54 from the archaeon Acidianus ambivalens and its comparison with related structures suggests a model for the SRP-SRP receptor complex.
Differences in the conserved consensus regions for nucleotide binding and the subdomain interfaces are observed, which provide information about the regulation of the GTPase, and allow a common signalling mechanism for the SRP-SR system to be proposed.