Domain structure, GTP-hydrolyzing activity and 7S RNA binding of Acidianus ambivalens ffh-homologous protein suggest an SRP-like complex in archaea.

@article{Moll1999DomainSG,
  title={Domain structure, GTP-hydrolyzing activity and 7S RNA binding of Acidianus ambivalens ffh-homologous protein suggest an SRP-like complex in archaea.},
  author={Ralf G Moll and S Schmidtke and Günter Schäfer},
  journal={European journal of biochemistry},
  year={1999},
  volume={259 1-2},
  pages={
          441-8
        }
}
In this study we provide, for the first time, experimental evidence that a protein homologous to bacterial Ffh is part of an SRP-like ribonucleoprotein complex in hyperthermophilic archaea. The gene encoding the Ffh homologue in the hyperthermophilic archaeote Acidianus ambivalens has been cloned and sequenced. Recombinant Ffh protein was expressed in E. coli and subjected to biochemical and functional studies. A. ambivalens Ffh encodes a 50.4-kDa protein that is structured by three distinct… 
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.
TLDR
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.
An archaeal protein homologous to mammalian SRP54 and bacterial Ffh recognizes a highly conserved region of SRP RNA
TLDR
The gene encoding the 54 kDa protein of signal recognition particle (SRP54) in the hyperthermophilic archaeon Pyrococcus furiosus has been cloned and sequenced and the RNA binding properties of the purified protein were determined by filter binding assays.
Protein-protein, protein-RNA and protein-lipid interactions of signal-recognition particle components in the hyperthermoacidophilic archaeon Acidianus ambivalens.
  • R. Moll
  • Biology, Medicine
    The Biochemical journal
  • 2003
TLDR
Under in vitro conditions, recombinantly generated Ffh and FtsY associate in a nucleotide-independent manner, supporting a structural receptor model with two interacting apoproteins, suggesting an equilibrium of soluble and membrane-bound protein forms under in vivo conditions.
Crystallization and preliminary x-ray diffraction studies on the conserved GTPase domain of the signal recognition particle from Acidianus ambivalens.
TLDR
Crystallization experiments of the native protein as well as of the Thr112Ala mutant, which is deficient in GTP hydrolysis, resulted in crystals suitable for X-ray diffraction, which produced Selenomethionine protein, which was produced.
Identification and characterization of Streptococcus pneumoniae Ffh, a homologue of SRP54 subunit of mammalian signal recognition particle.
  • F. Zheng, C. Zook, +4 authors S. Peng
  • Medicine, Biology
    Biochemical and biophysical research communications
  • 2002
TLDR
The Ffh, a homologue of the mammalian SRP54 subunit from S. pneumoniae, is identified and resulted in a 20-fold stimulation in GTP hydrolysis and a similar GTPase stimulation is also observed between F fh-NG and FtsY, suggesting that the NG domain is sufficient and the M domain is not required for GTPasing.
In Vivo Analysis of an Essential Archaeal Signal Recognition Particle in Its Native Host
TLDR
Copurification studies will provide insight into the significance of the similarities and differences of the protein-targeting systems of the three domains of life, thereby increasing knowledge about the recognition of translocated proteins in general.
Purification and Characterization of the N-Terminal Domain of ExeA: a Novel ATPase Involved in the Type II Secretion Pathway of Aeromonas hydrophila
TLDR
Findings support a model whereby ExeAB utilizes energy derived from ATP hydrolysis to facilitate the correct localization and multimerization of the ExeD secretin.
Archaea Signal Recognition Particle Shows the Way
TLDR
Comparative analyses of the archaea genomes and their SRP component sequences, combined with structural and biochemical data, support a prominent role of the SRP RNA in the assembly and function of the Archaea SRP.
Functional Characterization of an Extremely Thermophilic ATPase in Membranes of the Crenarchaeon Acidianus ambivalens
Abstract A plasma membrane-bound adenosine triphosphatase with specific activities up to 0.2 μmol min−1 (mg protein)−1 at 80°C was detected in the thermoacidophilic crenarchaeon Acidianus ambivalens
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TLDR
Two adjacent genes of the acidophilic and hyperthermophilic crenarchaeon Acidianus ambivalens were cloned and sequenced and the deletion mutant protein SR alpha lacking the hydrophilic H-region displays a higher GTP-hydrolyzing activity when compared to the unmodified recombinant protein.
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TLDR
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TLDR
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TLDR
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