Signal Sequence Cleavage of Peptidyl-tRNA Prior to Release from the Ribosome and Translocon

Many secretory polypeptides undergo cleavage of their signal sequence. In this study, we observed and quantitated the presence of a tRNA-bound, ribosome-associated polypeptide subpopulation present in vitro. This subpopulation was accessible to signal peptidase on ribosome-associated polypeptides lo...

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Bibliographic Details
Published in:The Journal of biological chemistry 2004-06, Vol.279 (24), p.24919-24922
Main Authors: Wollenberg, Michael S., Simon, Sanford M.
Format: Article
Language:English
Subjects:
beta-Lactamases - genetics
beta-Lactamases - metabolism
Endoplasmic Reticulum - metabolism
Molecular Weight
Protein Biosynthesis
Protein Sorting Signals - physiology
Protein Transport
Ribosomes - metabolism
RNA, Transfer, Amino Acyl - metabolism
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Summary:Many secretory polypeptides undergo cleavage of their signal sequence. In this study, we observed and quantitated the presence of a tRNA-bound, ribosome-associated polypeptide subpopulation present in vitro. This subpopulation was accessible to signal peptidase on ribosome-associated polypeptides longer than 114 amino acids. This demonstrates that it is possible for a peptidyl-tRNA species, in the midst of translation, to be processed by the endoplasmic reticulum signal peptidase implying that the peptidase is closely associated with the mammalian translocon.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.C400018200