한빛사 논문
Abstract
Heon-Ki Kim,1,3 Ryu-Ryun Kim,1,3 Jang-Hyun Oh,2 Hanna Cho,1 Alexander Varshavsky,2,* and Cheol-Sang Hwang1,*
1Department of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk 790-784, South Korea
2Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125, USA
3These authors contributed equally to this work
*Correspondence: A.V., C.-S.H.
http://dx.doi.org/10.1016/j.cell.2013.11.031
Summary
The Arg/N-end rule pathway targets for degradation proteins that bear specific unacetylated N-terminal residues while the Ac/N-end rule pathway targets proteins through their Nα-terminally acetylated (Nt-acetylated) residues. Here, we show that Ubr1, the ubiquitin ligase of the Arg/N-end rule pathway, recognizes unacetylated N-terminal methionine if it is followed by a hydrophobic residue. This capability of Ubr1 expands the range of substrates that can be targeted for degradation by the Arg/N-end rule pathway because virtually all nascent cellular proteins bear N-terminal methionine. We identified Msn4, Sry1, Arl3, and Pre5 as examples of normal or misfolded proteins that can be destroyed through the recognition of their unacetylated N-terminal methionine. Inasmuch as proteins bearing the Nt-acetylated N-terminal methionine residue are substrates of the Ac/N-end rule pathway, the resulting complementarity of the Arg/N-end rule and Ac/N-end rule pathways enables the elimination of protein substrates regardless of acetylation state of N-terminal methionine in these substrates.
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