E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle.
E. coli 4.5S RNA and P48 have been shown to be homologous to SRP7S RNA and SRP54, respectively. Here we report that expression of human SRP7S in E. coli can suppress the lethality caused by depletion of 4.5S RNA. In E. coli, both RNAs are associated with P48. In vitro, both E. coli P48 and SRP54 specifically bind to 4.5S RNA. Strains depleted of 4.5S RNA strongly accumulate pre-beta-lactamase and fail to accumulate maltose binding protein. These effects commence well before any growth defect is observed and are suppressed by expression of human SRP7S. Strains overproducing P48 also accumulate pre-beta-lactamase. 4.5S RNA and P48 are components of a ribonucleoprotein particle that we propose to be required for the secretion of some proteins.
Ribes
V
V
European Molecular Biology Laboratory, Heidelberg, Federal Republic of Germany.
Römisch
K
K
Giner
A
A
Dobberstein
B
B
Tollervey
D
D
D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics*; D005822:Genetic Vectors; D006801:Humans; D008957:Models, Genetic; D011485:Protein Binding; D012261:Ribonucleoproteins / Q000235:genetics*; D012270:Ribosomes / Q000378:metabolism; D018271:Signal Recognition Particle; D013489:Suppression, Genetic; D001618:beta-Lactamases / Q000235:genetics
D012261:Ribonucleoproteins; D018271:Signal Recognition Particle; D001618:beta-Lactamases