The signal recognition particle receptor alpha subunit of the hyperthermophilic archaeon Acidianus ambivalens exhibits an intrinsic GTP-hydrolyzing activity.

@article{Moll1997TheSR,
  title={The signal recognition particle receptor alpha subunit of the hyperthermophilic archaeon Acidianus ambivalens exhibits an intrinsic GTP-hydrolyzing activity.},
  author={Ralf G Moll and S Schmidtke and Arnd Petersen and Günter Schäfer},
  journal={Biochimica et biophysica acta},
  year={1997},
  volume={1335 1-2},
  pages={
          218-30
        }
}
Domain structure, GTP-hydrolyzing activity and 7S RNA binding of Acidianus ambivalens ffh-homologous protein suggest an SRP-like complex in archaea.
TLDR
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.
Protein-protein, protein-RNA and protein-lipid interactions of signal-recognition particle components in the hyperthermoacidophilic archaeon Acidianus ambivalens.
  • R. Moll
  • Biology
    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.
The Archaeal Signal Recognition Particle: Steps Toward Membrane Binding
  • R. Moll
  • Biology
    Journal of bioenergetics and biomembranes
  • 2004
TLDR
Investigations of the archaeal SRP pathway could identify novel aspects of this process not previously reported or unique to archaea when compared with the respective eukaryal and bacterial systems.
X‐ray structure of the T. Aquaticus Ftsy:GDP complex suggests functional roles for the C‐terminal helix of the SRP GTPases
TLDR
The structure of the monomeric protein reveals, unexpectedly, canonical binding interactions for GDP and is compared to Ffh NG, suggesting distinct mechanisms by which the interactions of the NG domain “module” are regulated in the context of the two SRP GTPases.
Induced nucleotide specificity in a GTPase
  • S. Shan, P. Walter
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 2003
TLDR
This work shows that, unlike other GTPases, free FtsY exhibits only low preference for GTP over other nucleotides, and proposes that this conformational change leads to more accurate positioning of the nucleotide and thus could contribute to activation of Ftsy's GTPase activity by a novel mechanism.
Archaeal protein translocation crossing membranes in the third domain of life.
  • J. Eichler
  • Biology
    European journal of biochemistry
  • 2000
TLDR
Understanding archaealprotein translocation could reveal the universal nature of certain features of protein translocation which, in some cases, may not be readily obvious from current comparisons of bacterial and eukaryotic systems.
The signal recognition particle of Archaea.
The Hyper-Thermostable Fe-Superoxide Dismutase from the Archaeon Acidianus ambivalens: Characterization, Recombinant Expression, Crystallization and Effects of Metal Exchange
TLDR
An iron-containing superoxide dismutase of the hyperthermophilic archaeon Acidianus ambivalens has been purified and characterized and the gene has been cloned and sequenced, and both the native and the heterologously overproduced protein turned out to have extraordinarily high melting temperatures.
Protein transport across and into cell membranes in bacteria and archaea
TLDR
The different systems employed to translocate and insert proteins across or into the cytoplasmic membrane of archaea and bacteria are described.
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References

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A putative signal recognition particle receptor α subunit (SRα) homologue is expressed in the hyperthermophilic crenarchaeon Sulfolobus acidocaldarius
TLDR
A 1.64 kb genomic DNA sequence from the hyperthermophilic crenarchaeon Sulfolobus acidocaldarius is composed of two adjacent genes that encodes the putative signal recognition particle receptor α subunit (SRα) and the main transcript of orf-1 appears as a monocistronic RNA in Northern hybridization.
srb: a Bacillus subtilis gene encoding a homologue of the alpha-subunit of the mammalian signal recognition particle receptor.
TLDR
A defect in srb inhibited cell growth and protein translocation and showed than an amphipathic alpha-helix is positioned in the N-terminal region of the putative B. subtilis protein.
GTPase activity of a bacterial SRP-like complex.
TLDR
It is demonstrated that the SRPM54 protein has an intrinsic GTPase activity in vitro and kinetic parameters for the enzymatic reaction have been determined.
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TLDR
It is shown that the P48/4.5S RNA ribonucleoprotein complex interacts specifically with the signal sequence of a nascent secretory protein and therefore is a signal recognition particle.
Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor
TLDR
It is shown that the E. coli Ffh/4.5S ribonucleoprotein binds tightly to FtsY in a GTP-dependent manner which results in the stimulation of GTP hydrolysis which can be inhibited by synthetic signal peptides.
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TLDR
This analysis provides insight into the significance of structural variation in SRP RNA and identifies novel conserved motifs in protein components of this pathway, and hypothesizes that a component of the Srp68/72p heterodimer serves as the GDS for both Srp54p and SR alpha.
An Amino-terminal Domain Containing Hydrophobic and Hydrophilic Sequences Binds the Signal Recognition Particle Receptor α Subunit to the β Subunit on the Endoplasmic Reticulum Membrane (*)
TLDR
Extraction of microsomal SRα at high pH supplemented with 1 M NaSCN suggests that SRα and the membrane binding domain are not integrated in the endoplasmic reticulum membrane.
A gene in the archaebacterium Sulfolobus solfataricus that codes for a protein equivalent to the alpha subunits of the signal recognition particle receptor in eukaryotes
We have sequenced a gene in the archaebacterium Sulfolobus solfataricus that codes for a protein that shows sequence similarity to the alpha subunit of the signal recognition particle receptor or
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