Yes / The ribosome exit site is a focal point for the interaction of protein-biogenesis factors that guide the fate of nascent polypeptides. These factors include chaperones such as NAC, N-terminal-modifying enzymes like Methionine aminopeptidase (MetAP), and the signal recognition particle (SRP), which targets secretory and membrane proteins to the ER. These
factors potentially compete with one another in the short time-window when the nascent chain first emerges at the exit
site, suggesting a need for regulation. Here, we show that MetAP contacts the ribosome at the universal adaptor site
where it is adjacent to the α subunit of NAC. SRP is also known to contact the ribosome at this site. In the absence of
NAC, MetAP and SRP antagonize each other, indicating a novel role for NAC in regulating the access of MetAP and
SRP to the ribosome. NAC also functions in SRP-dependent targeting and helps to protect substrates from aggregation
before translocation. / This work was supported by grants from the BBSRC [H007202/1] and Wellcome Trust [097820/Z/11/A].
| Identifer | oai:union.ndltd.org:BRADFORD/oai:bradscholars.brad.ac.uk:10454/17895 |
| Date | 10 June 2020 |
| Creators | Nyathi, Yvonne, Pool, M.R. |
| Source Sets | Bradford Scholars |
| Language | English |
| Detected Language | English |
| Type | Article, Published version |
| Rights | © 2015 Nyathi and Pool. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/)., CC-BY-NC-SA |
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