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Nucleic Acids Research, 1994, Vol. 22, No. 11 2028-2035
© 1994

MOLECULAR BIOLOGY

The heterodimeric subunit SRP9/14 of the signal recognition particle functions as permuted single polypeptide chain

Fabrice Bovia, Nazarena Bui and Katharina Strub*

Département de Biologie Cellulaire, Université de Genève Sciences III, CH-1211 Geneva 4, Switzerland

*To whom correspondence should be addressed

Received March 11, 1994. Revised May 11, 1994. Accepted May 11, 1994.

The targeting of nascent polypeptide chains to the endoplasmic reticulum is mediated by a cytoplasmic ribonucleoprotein, the signal recognition particle (SRP). The 9 kD (SRP9) and the 14 kD (SRP14) subunits of SRP are required to confer elongation arrest activity to the particle. SRP9 and SRP14 form a heterodimer which specifically binds to SRP RNA. We have constructed cDNAs that encode single polypeptide chains comprising SRP9 and SRP14 sequences in the two possible permutations linked by a 17 amino acid peptide. We found that both fusion proteins specifically bound to SRP RNA as monomeric molecules folded into a heterodimer-like structure. Our results corroborate the previous hypothesis that the authentic heterodimer binds to SRP RNA in equimolar ratio. In addition, both fusion proteins conferred elongation arrest activity to SRP(–9/14), which lacks this function, and one fusion protein could functionally replace the heterodimer in the translocation assay. Thus, the normal N-and C-termini of both proteins have no essential role in folding, RNA-binding and in mediating the biological activities. The possibility to express the heterodimeric complex as a single polypeptide chain facilitates the analysis of its functions and its structure in vivo and in vitro.


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