The P124A mutation of SRP14 alters its migration on SDS-PAGE without impacting its function
Author:
Publisher
China Science Publishing & Media Ltd.
Subject
General Medicine,Biochemistry,Biophysics,Molecular Biology
Link
https://engine.scichina.com/doi/pdf/57F2BBB5FAF24A74A803D9491E922B00
Reference19 articles.
1. Akopian D, Shen K, Zhang X, Shan S. Signal recognition particle: an essential protein-targeting machine. Annu Rev Biochem, 2013, 82: 693-721.
2. Siegel V, Walter P. Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane. J Cell Biol, 1985, 100: 1913-1921.
3. Weichenrieder O, Wild K, Strub K, Cusack S. Structure and assembly of the Alu domain of the mammalian signal recognition particle. Nature, 2000, 408: 167-173.
4. Mary C, Scherrer A, Huck L, Lakkaraju AKK, Thomas Y, Johnson AE, Strub K. Residues in SRP9/14 essential for elongation arrest activity of the signal recognition particle define a positively charged functional domain on one side of the protein. RNA, 2010, 16: 969-979.
5. Lakkaraju AKK, Mary C, Scherrer A, Johnson AE, Strub K. SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites. Cell, 2008, 133: 440-451.
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