Abstract:
:The ubiquitin-like modifier, FAT10, is involved in proteasomal degradation and antigen processing. As ubiquitin and the ubiquitin-like modifier, ISG15, cotranslationally modify proteins, we investigated whether FAT10 could also be conjugated to newly synthesized proteins. Indeed, we found that nascent proteins are modified with FAT10, but not with the same preference for newly synthesized proteins as observed for ISG15. Our data show that puromycin-labeled polypeptides are strongly modified by ISG15 and less intensely by ubiquitin and FAT10. Nevertheless, conjugates of all three modifiers copurify with ribosomes. Taken together, we show that unlike ISG15, ubiquitin and FAT10 are conjugated to a similar degree to newly translated and pre-existing proteins.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Spinnenhirn V,Bitzer A,Aichem A,Groettrup Mdoi
10.1002/1873-3468.12512subject
Has Abstractpub_date
2017-01-01 00:00:00pages
186-195issue
1eissn
0014-5793issn
1873-3468journal_volume
591pub_type
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