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Analysis of the interplay of protein biogenesis factors at the ribosome exit site reveals new role for NAC

Nyathi, Yvonne
; 
Pool, M.R.
Publication Date
2015-07
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Keywords
Protein biogenesis, Protein targeting, Protein translocation, Ribosome, Signal recognition particle, NAC
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/).
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openAccess
Accepted for publication
2015-06-03
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Life Sciences Publications
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Abstract
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.
URI
http://hdl.handle.net/10454/17895
Version
Published version
Citation
Nyathi Y and Pool MR (2015) Analysis of the interplay of protein biogenesis factors at the ribosome exit site reveals new role for NAC. Journal of Cell Biology. 210(2): 287-301.
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Link to Version of Record
https://doi.org/10.1083/jcb.201410086
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Article
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