Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway
Significance We found that the yeast Hsp90 chaperone system is greatly impaired in naa10Δ cells, which cannot N-terminally acetylate a majority of normally N-terminally acetylated proteins, including Hsp90 and its cochaperones. Hsp90 clients, including Chk1, Kar4, Tup1, Gpd1, Ste11, and even the Hsp...
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Hlavní autoři: | , , |
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Médium: | Artigo |
Jazyk: | angličtina |
Vydáno: |
2017
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On-line přístup: | https://doi.org/10.1073/pnas.1705898114 https://www.pnas.org/content/pnas/114/22/E4370.full.pdf |
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