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Nucleic Acids Research, 1994, Vol. 22, No. 13 2557-2567
© 1994

RNA

Genetic and biochemical analysis of the fission yeast ribonucleoprotein particle containing a homolog of Srp54p

David Selinger+, Patrick Brennwald§, Steven Althoff, Claudia Reich, Byron Hann1, Peter Walter1 and Jo Ann Wise*

Department of Biochemistry, University of Illinois at Urbana-Champaign Urbana, IL 61801 1Department of Biochemistry, University of California at San Francisco San Francisco, CA 94143, USA

*To whom correspondence should be addressed at: University of Illinois, Department of Biochemistry, 318 Roger Adams Laboratory, 600 South Matthews Avenue, Urbana, IL 61801, USA

Received March 31, 1994. Revised June 1, 1994. Accepted June 1, 1994.

Mammalian signal recognition particle (SRP), a complex of six polypeptides and one 7SL RNA molecule, is required for targeting nascent presecretory proteins to the endoplasmic reticulum (ER). Earlier work identified a Schizosaccharomyces pombe homolog of human SRP RNA and showed that it is a component of a particle similar in size and biochemical properties to mammalian SRP. The recent cloning of the gene encoding a fission yeast protein homologous to Srp54p has made possible further characterization of the subunit structure, subcellular distribution, and assembly of fission yeast SRP. S.pombe SRP RNA and Srp54p co-sediment on a sucrose velocity gradient and coimmunoprecipitate, indicating that they reside in the same complex. In vitro assays demonstrate that fission yeast Srp54p binds under stringent conditions to E.coli SRP RNA, which consists essentially of domain IV, but not to the full-length cognate RNA nor to an RNA in which domain III has been deleted in an effort to mirror the structure of bacterial homologs. Moreover, the association of S.pombe Srp54p with SRP RNA in vivo is disrupted by conditional mutations not only in domain IV, which contains its binding site, but in domains I and III, suggesting that the particle may assemble cooperatively. The growth defects conferred by mutations throughout SRP RNA can be suppressed by overexpression of Srp54p, and the degree to which growth is restored correlates inversely with the severity of the reduction in protein binding. Conditional mutations in SRP RNA also reduce its sedimentation with the ribosome/membrane pellet during cell fractionation. Finally, immunoprecipitation under native conditions of an SRP-enriched fraction from [35S]-labeled fission yeast cells suggests that five additional polypeptides are complexed with Srp54p; each of these proteins is similar in size to a constituent of mammalian SRP, implying that the subunit structure of this ribonucleoprotein is conserved over vast evolutionary distances.

+Present addresses: Institute of Molecular Biology, University of Oregon, Eugene, OR 97403

§Present addresses: Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510, USA


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