Protein SRP54 of human signal recognition particle: Cloning, expression, and comparative analysis of functional sites Journal Article


Authors: Gowda, K.; Black, S. D.; Moeller, I.; Sakakibara, Y.; Liu, M. C.; Zwieb, C.
Article Title: Protein SRP54 of human signal recognition particle: Cloning, expression, and comparative analysis of functional sites
Abstract: Signal recognition particle (SRP) plays a critical role in the targeting of secretory proteins to cellular membranes. An essential component of SRP is the protein SRP54, which interacts not only with the nascent signal peptide, but also with the SRP RNA. To understand better how protein targeting occurs in the human system, the human SRP54 gene was cloned, sequenced, and the protein was expressed in bacteria and insect cells. Recombinant SRP54 was purified from both sources. The protein bound to SRP RNA in the presence of protein SRP19, and associated with the signal peptide of in vitro translated pre-prolactin. Comparative sequence analysis of human SRP54 with homologs from all three phylogenetic domains was combined with high-stringency protein secondary structure prediction. A conserved RNA-binding loop was predicted in the largely helical M-domain of SRP54. Contrary to general belief, the unusually high number of methionine residues clustered outside the predicted helices, thus indicating a mechanism of signal peptide recognition that may involve methionine-rich loops.
Keywords: signal transduction; animals; gene expression; protein targeting; cell line; protein binding; rna binding protein; rna; molecular cloning; cloning, molecular; rna-binding proteins; amino acid sequence; molecular sequence data; sequence homology, amino acid; signal peptide; escherichia coli; recombinant proteins; protein secretion; spodoptera; binding sites; protein secondary structure; protein structure, secondary; phylogeny; prolactin; docking protein; insecta; signal recognition particle; humans; human; priority journal; article; rna-protein interactions
Journal Title: Gene
Volume: 207
Issue: 2
ISSN: 0378-1119
Publisher: Elsevier Science, Inc.  
Date Published: 1998-01-30
Start Page: 197
End Page: 207
Language: English
DOI: 10.1016/s0378-1119(97)00627-6
PUBMED: 9511762
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 12 December 2016 -- Source: Scopus
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