Literature DB >> 2460823

Isolation and characterization of a cDNA clone encoding the 19 kDa protein of signal recognition particle (SRP): expression and binding to 7SL RNA.

K Lingelbach1, C Zwieb, J R Webb, C Marshallsay, P J Hoben, P Walter, B Dobberstein.   

Abstract

Signal recognition particle (SRP) consists of a 7SL RNA molecule and 6 protein subunits. We have isolated and characterized cDNA clones from human liver which encode the 19kDa protein subunit (SRP19). This subunit binds to the RNA directly and mediates binding of a second polypeptide, the 54kDa subunit which is involved in signal sequence recognition. Amino acid sequences deduced from the human cDNA sequence were identical to amino acid sequences of tryptic peptides from canine pancreatic SRP19. In vitro transcription and translation of the human cDNA resulted in a protein product the same size as canine SRP19 which could be immunoprecipitated by an antiserum raised against canine SRP19. SRP19 synthesized in a cell-free system specifically bound to 7SL RNA. The sequence of SRP19 is discussed with respect to its binding to 7SL RNA.

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Year:  1988        PMID: 2460823      PMCID: PMC338754          DOI: 10.1093/nar/16.20.9431

Source DB:  PubMed          Journal:  Nucleic Acids Res        ISSN: 0305-1048            Impact factor:   16.971


  30 in total

1.  The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle.

Authors:  T V Kurzchalia; M Wiedmann; A S Girshovich; E S Bochkareva; H Bielka; T A Rapoport
Journal:  Nature       Date:  1986 Apr 17-23       Impact factor: 49.962

2.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

3.  Isolation of microgram quantities of proteins from polyacrylamide gels for amino acid sequence analysis.

Authors:  M W Hunkapiller; E Lujan; F Ostrander; L E Hood
Journal:  Methods Enzymol       Date:  1983       Impact factor: 1.600

4.  Primary structure of human nuclear ribonucleoprotein particle C proteins: conservation of sequence and domain structures in heterogeneous nuclear RNA, mRNA, and pre-rRNA-binding proteins.

Authors:  M S Swanson; T Y Nakagawa; K LeVan; G Dreyfuss
Journal:  Mol Cell Biol       Date:  1987-05       Impact factor: 4.272

5.  Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities.

Authors:  M S Swanson; G Dreyfuss
Journal:  Mol Cell Biol       Date:  1988-05       Impact factor: 4.272

6.  Evidence for an extended 7SL RNA structure in the signal recognition particle.

Authors:  D W Andrews; P Walter; F P Ottensmeyer
Journal:  EMBO J       Date:  1987-11       Impact factor: 11.598

7.  7SL RNA from Schizosaccharomyces pombe is encoded by a single copy essential gene.

Authors:  V Ribes; P Dehoux; D Tollervey
Journal:  EMBO J       Date:  1988-01       Impact factor: 11.598

8.  Topological mapping of complement component C9 by recombinant DNA techniques suggests a novel mechanism for its insertion into target membranes.

Authors:  K K Stanley; J Herz
Journal:  EMBO J       Date:  1987-07       Impact factor: 11.598

9.  Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane.

Authors:  V Siegel; P Walter
Journal:  J Cell Biol       Date:  1985-06       Impact factor: 10.539

10.  Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle.

Authors:  R Gilmore; G Blobel; P Walter
Journal:  J Cell Biol       Date:  1982-11       Impact factor: 10.539

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  28 in total

1.  Assembly of the human signal recognition particle (SRP): overlap of regions required for binding of protein SRP54 and assembly control.

Authors:  J Yin; C H Yang; C Zwieb
Journal:  RNA       Date:  2001-10       Impact factor: 4.942

2.  Interaction of rice and human SRP19 polypeptides with signal recognition particle RNA.

Authors:  K Chittenden; K Gowda; S D Black; C Zwieb
Journal:  Plant Mol Biol       Date:  1997-06       Impact factor: 4.076

3.  Conformity of RNAs that interact with tetranucleotide loop binding proteins.

Authors:  C Zwieb
Journal:  Nucleic Acids Res       Date:  1992-09-11       Impact factor: 16.971

4.  Conserved tertiary base pairing ensures proper RNA folding and efficient assembly of the signal recognition particle Alu domain.

Authors:  Laurent Huck; Anne Scherrer; Lionel Terzi; Arthur E Johnson; Harris D Bernstein; Stephen Cusack; Oliver Weichenrieder; Katharina Strub
Journal:  Nucleic Acids Res       Date:  2004-09-21       Impact factor: 16.971

5.  Interaction of protein SRP19 with signal recognition particle RNA lacking individual RNA-helices.

Authors:  C Zwieb
Journal:  Nucleic Acids Res       Date:  1991-06-11       Impact factor: 16.971

6.  The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAs.

Authors:  F Bovia; M Fornallaz; H Leffers; K Strub
Journal:  Mol Biol Cell       Date:  1995-04       Impact factor: 4.138

Review 7.  Structure and function of signal recognition particle (SRP).

Authors:  K Römisch; V Ribes; S High; H Lütcke; D Tollervey; B Dobberstein
Journal:  Mol Biol Rep       Date:  1990       Impact factor: 2.316

8.  Determinants of a protein-induced RNA switch in the large domain of signal recognition particle identified by systematic-site directed mutagenesis.

Authors:  K Gowda; C Zwieb
Journal:  Nucleic Acids Res       Date:  1997-07-15       Impact factor: 16.971

9.  The Srp54 GTPase is essential for protein export in the fission yeast Schizosaccharomyces pombe.

Authors:  S M Althoff; S W Stevens; J A Wise
Journal:  Mol Cell Biol       Date:  1994-12       Impact factor: 4.272

10.  Structural and functional characterisation of the signal recognition particle-specific 54 kDa protein (SRP54) of tomato.

Authors:  S Krolkiewicz; H L Sänger; U Niesbach-Klösgen
Journal:  Mol Gen Genet       Date:  1994-12-01
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