
doi: 10.1515/bc.1999.021
pmid: 10195420
AbstractThe signal recognition particle (SRP), a ubiquitous cytoplasmic ribonucleoprotein particle, plays an essential role in promoting co-translational translocation of proteins into the endoplasmic reticulum. Here, we summarise recent progress made in the understanding of two essential SRP functions: the signal recognition function, which ensures the specificity, and the elongation arrest function, which increases the efficiency of translocation. Our discussion is based on functional data as well as on atomic structure information, both of which also support the notion that SRP is a very ancient particle closely related to ribosomes. Based on the significant increase of knowledge that has been accumulating on the structure of elongation factors and on their interactions with the ribosome, we speculate about a possible mechanism of the elongation arrest function.
570, Translation, Binding Sites, Evolution, Molecular Sequence Data, Translocation, Signal sequence, Methionine, RNA-protein, Alu Elements, Animals, Humans, RNA, Amino Acid Sequence, Ribosomes, Signal Recognition Particle, Signal Transduction, ddc: ddc:570
570, Translation, Binding Sites, Evolution, Molecular Sequence Data, Translocation, Signal sequence, Methionine, RNA-protein, Alu Elements, Animals, Humans, RNA, Amino Acid Sequence, Ribosomes, Signal Recognition Particle, Signal Transduction, ddc: ddc:570
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