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SRP54  -  signal recognition particle 54kDa

Canis lupus familiaris

 
 
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Disease relevance of SRP54

  • The recombinant SRP 54 kDa, which forms a ribonucleoprotein complex in E coli, was shown to bind to precursor proteins, but is unable to interact with the filamentous temperature-sensitive Y (Fts Y) membrane receptor of the translocation machinery [1].
 

High impact information on SRP54

  • These results strongly suggest that the Sec61 complex regulates the GTP hydrolysis cycle of the SRP-SR complex at the stage of signal sequence dissociation from SRP54 [2].
  • The SRP54 and SR alpha subunits of the signal recognition particle (SRP) and the SRP receptor (SR) undergo a tightly coupled GTPase cycle that mediates the signal sequence-dependent attachment of ribosomes to the Sec61 complex [3].
  • Empty site forms of the SRP54 and SR alpha GTPases mediate targeting of ribosome-nascent chain complexes to the endoplasmic reticulum [3].
  • Here we present the sequence of a complementary DNA clone of SRP54 which predicts a protein that contains a putative GTP-binding domain and an unusually methionine-rich domain [4].
  • Analysis of the primary amino acid sequence of one protein subunit of SRP (SRP54), as well as the alpha subunit of the SRP receptor (SR alpha), has indicated that these proteins contain predicted GTP binding sites [5].
 

Biological context of SRP54

  • Hydrolysis by both SRP54 and SR alpha is a prerequisite for dissociation of the SRP-SR complex [3].
 

Other interactions of SRP54

  • The binding affinity of SRP68/72 for SRP RNA-Fl was unaffected by the presence of SRP9/14, and hence the binding of the heterodimers to SRP RNA is noncooperative in the absence of SRP54 and SRP19 [6].
 

Analytical, diagnostic and therapeutic context of SRP54

  • To identify the domain or site on SRP54 that interacts with the signal sequence we used a photocross-linking approach followed by limited proteolysis and immunoprecipitation using anti-peptide antibodies specific for defined regions of SRP54 [7].

References

 
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