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Gene Review

SRP19  -  signal recognition particle 19kDa

Homo sapiens

Synonyms: Signal recognition particle 19 kDa protein
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Disease relevance of SRP19

  • Finally, SRP19 bound specifically not only to SRP RNA but also to the A-form of Escherichia coli 5S ribosomal RNA, thereby indicating structural similarities between these two RNA molecules [1].

High impact information on SRP19

  • During assembly of the SRP, binding of SRP19 precedes and promotes the association of SRP54 (refs 4, 5) [2].
  • Here we report the 1.8 angstrom resolution crystal structure of human SRP19 in complex with its primary binding site on helix 6 of SRP RNA, which consists of a stem-loop structure closed by an unusual GGAG tetraloop [3].
  • We have determined the crystal structure of Methanococcus jannaschii SRP19 bound to the S domain of human 7SL RNA at 2.9 A resolution [4].
  • Furthermore, we found that the alternative splicing involving the 19 kDa protein of signal recognition particle (SRP19) gene, that is known to occur at exon 14 of APC, is also controlled in a tissue-specific manner, and one type of transcript lacked in some organs [5].
  • Although transportin is known to import a variety of proteins, SRP19 import is the first function assigned to importin 8 [6].

Chemical compound and disease context of SRP19

  • In order to have a convenient source for the purification of milligram amounts of SRP19, we expressed in Escherichia coli a human SRP19 cDNA with an amino-terminal addition of six histidine residues [7].

Biological context of SRP19


Anatomical context of SRP19


Associations of SRP19 with chemical compounds

  • Activities of the chimeric RNAs were measured with respect to protein SRP19 and the methionine-rich RNA-binding domain of protein SRP54 (SRP54M) [13].
  • Changing A213 and A214 to a uridine has no effect on the SRP19-dependent binding of SRP54M [13].
  • The absence of SRP19 did, however, increase membrane bacterioruberin levels [12].
  • Using site-directed mutagenesis we demonstrate that the two arginine residues of the EGRR motif conserved in all SRP19 homologues are essential for SRP activity [14].
  • The histidine-tagged SRP19 bound specifically to a 150-nucleotide RNA derived from SRP RNA, with an apparent Kd of 1 nM, and bound, with greatly reduced affinity, to a mutagenized form of the SRP RNA derivative that contained an altered helix 6 tetranucleotide loop [7].

Physical interactions of SRP19

  • Hence, the crystal structure of the ternary complex suggests why SRP19 is necessary for the stable binding of SRP54 to the S domain RNA [15].

Other interactions of SRP19

  • The structure explains the role of SRP19 and provides a molecular framework for SRP54 binding and SRP assembly in Eukarya and Archaea [2].
  • Here we present the crystal structure of a human SRP ternary complex consisting of SRP19, the M domain of SRP54 and the S domain of 7SL RNA [15].
  • A group of RNA binding proteins, termed tetraloop binding proteins, includes ribosomal protein S15 and protein SRP19 of signal recognition particle [16].

Analytical, diagnostic and therapeutic context of SRP19


  1. Cooperative assembly of signal recognition particle RNA with protein SRP19. Walker, K.P., Black, S.D., Zwieb, C. Biochemistry (1995) [Pubmed]
  2. Structure of the SRP19 RNA complex and implications for signal recognition particle assembly. Hainzl, T., Huang, S., Sauer-Eriksson, A.E. Nature (2002) [Pubmed]
  3. Crystal structure of an early protein-RNA assembly complex of the signal recognition particle. Wild, K., Sinning, I., Cusack, S. Science (2001) [Pubmed]
  4. Crystal structure of SRP19 in complex with the S domain of SRP RNA and its implication for the assembly of the signal recognition particle. Oubridge, C., Kuglstatter, A., Jovine, L., Nagai, K. Mol. Cell (2002) [Pubmed]
  5. Multiple forms of the APC gene transcripts and their tissue-specific expression. Horii, A., Nakatsuru, S., Ichii, S., Nagase, H., Nakamura, Y. Hum. Mol. Genet. (1993) [Pubmed]
  6. Signal recognition particle protein 19 is imported into the nucleus by importin 8 (RanBP8) and transportin. Dean, K.A., von Ahsen, O., Görlich, D., Fried, H.M. J. Cell. Sci. (2001) [Pubmed]
  7. Purification and biochemical characterization of the 19-kDa signal recognition particle RNA-binding protein expressed as a hexahistidine-tagged polypeptide in Escherichia coli. Henry, K.A., Zwieb, C., Fried, H.M. Protein Expr. Purif. (1997) [Pubmed]
  8. Isolation and characterization of a cDNA clone encoding the 19 kDa protein of signal recognition particle (SRP): expression and binding to 7SL RNA. Lingelbach, K., Zwieb, C., Webb, J.R., Marshallsay, C., Hoben, P.J., Walter, P., Dobberstein, B. Nucleic Acids Res. (1988) [Pubmed]
  9. S-domain assembly of the signal recognition particle. Sauer-Eriksson, A.E., Hainzl, T. Curr. Opin. Struct. Biol. (2003) [Pubmed]
  10. Solution structure of protein SRP19 of Archaeoglobus fulgidus signal recognition particle. Pakhomova, O.N., Deep, S., Huang, Q., Zwieb, C., Hinck, A.P. J. Mol. Biol. (2002) [Pubmed]
  11. Assembly of the human signal recognition particle (SRP): overlap of regions required for binding of protein SRP54 and assembly control. Yin, J., Yang, C.H., Zwieb, C. RNA (2001) [Pubmed]
  12. SRP19 Is a Dispensable Component of the Signal Recognition Particle in Archaea. Yurist, S., Dahan, I., Eichler, J. J. Bacteriol. (2007) [Pubmed]
  13. Two strategically placed base pairs in helix 8 of mammalian signal recognition particle RNA are crucial for the SPR19-dependent binding of protein SRP54. Yin, J., Yang, C.H., Zwieb, C. RNA (2004) [Pubmed]
  14. Isolation and cloning of the Yarrowia lipolytica SEC65 gene, a component of the yeast signal recognition particle displaying homology with the human SRP19 gene. Sánchez, M., Beckerich, J.M., Gaillardin, C., Domínguez, A. Gene (1997) [Pubmed]
  15. Induced structural changes of 7SL RNA during the assembly of human signal recognition particle. Kuglstatter, A., Oubridge, C., Nagai, K. Nat. Struct. Biol. (2002) [Pubmed]
  16. Conformity of RNAs that interact with tetranucleotide loop binding proteins. Zwieb, C. Nucleic Acids Res. (1992) [Pubmed]
  17. Systematic site-directed mutagenesis of protein SRP19. Identification of the residues essential for binding to signal recognition particle RNA. Chittenden, K., Black, S.D., Zwieb, C. J. Biol. Chem. (1994) [Pubmed]
  18. Identification of an RNA-binding-loop in the N-terminal region of signal-recognition-particle protein SRP19. Black, S.D., Gowda, K., Chittenden, K., Walker, K.P., Zwieb, C. Eur. J. Biochem. (1997) [Pubmed]
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