Rad23 escapes degradation because it lacks a proteasome initiation region

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Rad23 escapes degradation because it lacks a proteasome initiation region

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Title: Rad23 escapes degradation because it lacks a proteasome initiation region
Author: Fishbain, Susan; Prakash, Sumit; Herrig, Annie; Elsasser, Suzanne; Matouschek, Andreas

Note: Order does not necessarily reflect citation order of authors.

Citation: Fishbain, Susan, Sumit Prakash, Annie Herrig, Suzanne Elsasser, and Andreas Matouschek. 2014. “Rad23 escapes degradation because it lacks a proteasome initiation region.” Nature communications 2 (1): 192. doi:10.1038/ncomms1194. http://dx.doi.org/10.1038/ncomms1194.
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Abstract: Rad23 is an adaptor protein that binds to both ubiquitinated substrates and to the proteasome. Despite its association with the proteasome, Rad23 escapes degradation. Here we show that Rad23 remains stable because it lacks an effective initiation region where the proteasome can engage the protein and unfold it. Rad23 contains several internal, unstructured loops but these are too short to act as initiation regions. Experiments with model proteins show that internal loops must be surprisingly long to engage the proteasome and support degradation. These length requirements are not specific to Rad23 and reflect a general property of the proteasome.
Published Version: doi:10.1038/ncomms1194
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4069258/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:12406741
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