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Mammalian and Escherichia coli signal recognition particles
Author(s) -
Luirink Joen,
Dobberstein Bernhard
Publication year - 1994
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1994.tb00284.x
Subject(s) - signal recognition particle , biology , signal recognition particle receptor , ribonucleoprotein , translation (biology) , protein targeting , escherichia coli , endoplasmic reticulum , rna , signal recognition particle rna , signal peptide , rna binding protein , microbiology and biotechnology , cytoplasm , protein sorting signals , membrane protein , ribosome , biochemistry , peptide sequence , gene , membrane , messenger rna
Summary Recent evidence from both biochemical and genetic studies indicates that protein targeting to the pro‐karyotic cytoplasmic membrane and the eukaryotic endoplasmic reticulum membrane may have more in common than previously thought. A ribonucleo‐protein 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 these 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.