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A further case of Dop‐ing in bacterial pupylation
Author(s) -
Bremm Anja,
Komander David
Publication year - 2010
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2010.149
Subject(s) - ubiquitin , function (biology) , computational biology , biology , posttranslational modification , microbiology and biotechnology , bacterial protein , bacteria , genetics , biochemistry , gene , enzyme
Two recent studies, one in this issue of EMBO reports and one in Molecular Cell, identify Dop as a depupylase, ascribing a novel function to Dop and providing further evidence for the functional similarity of the prokaryotic Pup‐modification system and the eukaryotic ubiquitin system.
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