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

Autor:	D.G. Kozlov, S.E. Cheperegin
Rok vydání:	2019
Předmět:	chemistry.chemical_compound Dipeptide Ecology Biochemistry Ubiquitin biology Chemistry biology.protein Processing Site Applied Microbiology and Biotechnology Biotechnology
Zdroj:	Biotekhnologiya. :25-29
ISSN:	2500-2341 0234-2758
DOI:	10.21519/0234-2758-2019-35-2-25-29
Popis:	It was shown that unlike eukaryotic ubiquitin-specific proteinases (DUBs deubiquitinating enzymes) deubiquitinase ElaD E.coli does not need obligatory presence of GlyGly dipeptide at the processing site and is capable to process sites GlyGly and GlyAla with equal efficiency. At the same time similar to eukaryotic DUB the bacterial enzyme does not process sites with dipeptides AlaGly, AlaAla or GlyPro. Considering functional mission of the deubiquitinating agent of E. coli, decrease in its specificity can be considered as valuable evolutional acquisition allowing to expand a list of the molecular targets being attacked during pathogenesis. ubiquitin, DUB, E. coli proteinase, elaD, virulence factor The authors sincerely thank the staff of the NRC «Kurchatov Institute» -GosNIIgenetika Drs. Skorokhodova A. Yu. and Goulevitch A.Yu. for designing and supplying the strain BL21(DE3)Ae/aD for the present work.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::1074f975ef5709313521275a36221c4d https://doi.org/10.21519/0234-2758-2019-35-2-25-29 Zobrazit plný text záznamu