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Signal recognition particle 54kDa

SRP54, Srp54p
54 kDa protein subunit of SRP that interacts with the signal peptide of secreted proteins (from NCBI)
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Top mentioned proteins: SRP19, CAN, ACID, HAD, V1a
Papers on SRP54
SRP-IgG detected incidentally associates with autoimmune myopathy.
Lennon et al., Rochester, United States. In Muscle Nerve, Dec 2015
Recombinant antigens confirmed SRP54-IgG-specificity alone (17), SRP72-IgG-specificity alone (3), both (32), neither (2).
Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions.
Beckmann et al., München, Germany. In Nat Struct Mol Biol, Oct 2015
The SRP comprises two subunits, 6S RNA and SRP54 or Ffh, and it facilitates elongation slowdown similarly to its eukaryotic counterpart.
Anti-signal recognition particle antibody in patients without inflammatory myopathy: a survey of 6180 patients with connective tissue diseases.
Kuwana et al., Tokyo, Japan. In Scand J Rheumatol, Sep 2015
The antibody against the 54-kDa protein of SRP (SRP54) was quantified by enzyme-linked immunosorbent assay (ELISA) in patients with anti-SRP antibody.
Molecular and Morphological Species Boundaries in the Gorgonian Octocoral Genus Pterogorgia (Octocorallia: Gorgoniidae).
Baker et al., Miami, United States. In Plos One, 2014
In order to test morphological species boundaries, and the validity of calyx and branch morphology as systematic characters, a phylogenetic analysis was undertaken utilizing partial gene fragments of three mitochondrial (mtMutS, cytochrome b, and igr4; 726bp total) and two nuclear (ITS2, 166bp; and SRP54 intron, 143bp) loci.
Circularization restores signal recognition particle RNA functionality in Thermoproteus.
Randau et al., Marburg an der Lahn, Germany. In Elife, 2014
Canonical SRP RNA genes have not been identified for some Thermoproteus species even though they contain SRP19 and SRP54 proteins.
Inefficient SRP interaction with a nascent chain triggers a mRNA quality control pathway.
Thomas et al., Dallas, United States. In Cell, 2014
Ago2 knockdown inhibited degradation of the mutant mRNA, while overexpression of Ago2 or knockdown of SRP54 promoted degradation of secretory protein mRNA.
Chromodomains read the arginine code of post-translational targeting.
Sinning et al., Heidelberg, Germany. In Nat Struct Mol Biol, 2012
The authors report the crystal structure of the chloroplast signal recognition particle (cpSRP) core from Arabidopsis thaliana, with the cpSRP54 tail comprising an arginine-rich motif bound to the second chromodomain of cpSRP43.
Recognition of a signal peptide by the signal recognition particle.
Nagai et al., Cambridge, United Kingdom. In Nature, 2010
A universally conserved component of SRP (refs 1, 2), SRP54 or its bacterial homologue, fifty-four homologue (Ffh), binds the signal peptides, which have a highly divergent sequence divisible into a positively charged n-region, an h-region commonly containing 8-20 hydrophobic residues and a polar c-region.
Archaea signal recognition particle shows the way.
Bhuiyan et al., Tyler, United States. In Archaea, 2009
Archaea SRP is composed of an SRP RNA molecule and two bound proteins named SRP19 and SRP54.
Protein targeting by the signal recognition particle.
Sinning et al., Heidelberg, Germany. In Biol Chem, 2009
SRP54 and FtsY, two multidomain proteins with guanosine triphosphatase (GTPase) activity, are the central elements of the SRP system.
Organized ribosome-containing structural domains in axons.
Koenig, Buffalo, United States. In Results Probl Cell Differ, 2008
Molecular markers concentrated in PARP domains include beta-actin mRNA, ZBP-1, SRP54, myosin Va and kinesin II molecular motor proteins.
Evolutionary substitution of two amino acids in chloroplast SRP54 of higher plants cause its inability to bind SRP RNA.
Schünemann et al., Bochum, Germany. In Febs Lett, 2008
The inability of Arabidopsis thaliana cpSRP54 to bind bacterial signal recognition particle-RNA is caused by two amino acid substitutions in the otherwise conserved RNA binding domain.
Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis.
van Wijk et al., Ithaca, United States. In Plant Physiol, 2008
cpSRP54 deletion led to a change in light-harvesting complex composition, an increase of PsbS, a decreased photosystem I/II ratio, and, in young leaves, to up-regulation of thylakoid proteases and stromal chaperones, including ClpC
Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43.
Sinning et al., Heidelberg, Germany. In Science, 2008
Secretory and membrane proteins carry amino-terminal signal sequences that, in cotranslational targeting, are recognized by the signal recognition particle protein SRP54 without sequence specificity.
Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA.
Shan et al., Pasadena, United States. In Mol Biol Cell, 2007
These results highlight intriguing differences between the classical and chloroplast SRP and SRP receptor GTPases, and help explain how the chloroplast SRP pathway can mediate efficient targeting of proteins to the thylakoid membrane.
Following the signal sequence from ribosomal tunnel exit to signal recognition particle.
Beckmann et al., München, Germany. In Nature, 2006
The signal sequence is presented at the ribosomal tunnel exit in an exposed position ready for accommodation in the hydrophobic groove of the rearranged SRP54 M domain.
A structural step into the SRP cycle.
Sinning et al., Heidelberg, Germany. In Mol Microbiol, 2004
The SRP core (SRP54 with its cognate RNA binding site) plays a central role in these interactions and communicates the different binding states by long-range interdomain communication.
Advances in the structure and functions of signal recognition particle in protein targeting.
Singh et al., Chandīgarh, India. In J Biol Regul Homeost Agents, 2003
GTPase activity of SRP54 releases SRP from SR.
Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor.
Blobel et al., New York City, United States. In Cell, 2003
This targeting step is regulated by three G proteins, SRP54, SR alpha, and SR beta, which act in concert.
Induced structural changes of 7SL RNA during the assembly of human signal recognition particle.
Nagai et al., Cambridge, United Kingdom. In Nat Struct Biol, 2002
crystal structure of a human SRP ternary complex consisting of SRP19, the M domain of SRP54 and the S domain of 7SL RNA
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