Changes in 7SL RNA conformation during the signal recognition particle cycle.
- 1 April 1991
- journal article
- research article
- Published by Springer Nature in The EMBO Journal
- Vol. 10 (4), 767-777
- https://doi.org/10.1002/j.1460-2075.1991.tb08008.x
Abstract
The structure of 7SL RNA has been probed by chemical modification followed by primer extension, using four substrates: (i) naked 7SL RNA; (ii) free signal recognition particle (SRP); (iii) polysome bound SRP; and (iv) membrane bound SRP. Decreasing sensitivity to chemical modification between these different substrates suggests regions on 7SL RNA that: bind proteins associated with SRP might interact with ribosomes; and are protected by binding to membranes. Other areas increase in chemical sensitivity, exemplified by a tertiary interaction present in naked 7SL RNA but not in free SRP. Such changes suggest that 7SL RNA changes its conformation during the SRP cycle. These conformational changes could be a necessary component to move through the SRP cycle from one stage to the next.Keywords
This publication has 61 references indexed in Scilit:
- Structural analysis of the peptidyl transferase region in ribosomal RNA of the eukaryote Xenopus laevisJournal of Molecular Biology, 1991
- Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: Analysis of biochemical mutants of SRPCell, 1988
- Mathematical modeling of the effects of the signal recognition particle on translation and translocation of proteins across the endoplasmic reticulum membraneJournal of Molecular Biology, 1987
- A 5 S rRNA-like secondary structure in the 7 SL RNA may define a ribosomal binding site of the signal recognition particleFEBS Letters, 1987
- The signal recognition particle receptor is a complex that contains two distinct polypeptide chains.The Journal of cell biology, 1986
- Interconversion of active and inactive 30 S ribosomal subunits is accompanied by a conformational change in the decoding region of 16 S rRNAJournal of Molecular Biology, 1986
- The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particleNature, 1986
- Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbantsCell, 1985
- Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein.The Journal of cell biology, 1981
- Structure and function of mammalian ribosomes: I. Isolation and characterization of active liver ribosomal subunitsJournal of Molecular Biology, 1970