Ubiquitin-Specific E. coli Proteinase Does Not Require the Obligatory Presence of Dipeptide GlyGly at Processing Site


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It is shown that, unlike eukaryotic ubiquitin-specific proteinases (deubiquitinating enzymes, DUBs), the E. coli deubiquitinase ElaD can process sites containing not only GlyGly but also GlyAla with equal efficiency. At the same time, the bacterial enzyme, like eukaryotic DUBs, fails to process sites containing AlaGly, AlaAla, or GlyPro dipeptides. In light of the functional mission of the E. coli deubiquitinating agent, its decreased specificity can be considered a valuable evolutional acquisition that allows expansion of the list of molecular targets attacked during pathogenesis.

作者简介

E. Sannikova

State Research Institute for Genetics and Selection of Industrial Microorganisms, Kurchatov Institute National Research Center (GosNIIgenetika, Kurchatov Institute NRC)

Email: dg_kozlov@genetika.ru
俄罗斯联邦, Moscow, 117545

S. Cheperegin

State Research Institute for Genetics and Selection of Industrial Microorganisms, Kurchatov Institute National Research Center (GosNIIgenetika, Kurchatov Institute NRC)

Email: dg_kozlov@genetika.ru
俄罗斯联邦, Moscow, 117545

D. Kozlov

State Research Institute for Genetics and Selection of Industrial Microorganisms, Kurchatov Institute National Research Center (GosNIIgenetika, Kurchatov Institute NRC)

编辑信件的主要联系方式.
Email: dg_kozlov@genetika.ru
俄罗斯联邦, Moscow, 117545

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