Mammalian and Escherichia coli signal recognition particles.
Recent evidence from both biochemical and genetic studies indicates that protein targeting to the prokaryotic cytoplasmic membrane and the eukaryotic endoplasmic reticulum membrane may have more in common than previously thought. A ribonucleoprotein particle was identified in Escherichia coli that consists of at least one protein (P48 or Ffh) and one RNA molecule (4.5S RNA), both of which exhibit strong sequence similarity with constituents of the mammalian signal recognition particle (SRP). Like the mammalian SRP, the E. coli SRP binds specifically to the signal sequence of presecretory proteins. Depletion of either P48 or 4.5S RNA affects translation and results in the accumulation of precursors of several secreted proteins. This review discusses the recent studies and speculates on the position of the SRP in the complex network of protein interactions involved in translation and membrane targeting in E. coli.
Luirink
J
J
Department of Microbiology, Biocentrum Amsterdam, The Netherlands.
Dobberstein
B
B
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D008954:Models, Biological; D014176:Protein Biosynthesis; D021382:Protein Sorting Signals / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D018271:Signal Recognition Particle / Q000737:chemistry / Q000378:metabolism*
D001426:Bacterial Proteins; D021382:Protein Sorting Signals; D011506:Proteins; D018271:Signal Recognition Particle