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

Ubiquitin-Specific E. coli Proteinase Does Not Require the Obligatory Presence of Dipeptide... ISSN 0003-6838, Applied Biochemistry and Microbiology, 2019, Vol. 55, No. 9, pp. 846–849. © Pleiades Publishing, Inc., 2019. Russian Text © The Author(s), 2019, published in Biotekhnologiya, 2019, Vol. 35, No. 2, pp. 25–29. PRODUCERS, BIOLOGY, SELECTION, AND GENE ENGINEERING Ubiquitin-Specif ic E. coli Proteinase Does Not Require the Obligatory Presence of Dipeptide GlyGly at Processing Site a a a, E. P. Sannikova , S. E. Cheperegin , and D. G. Kozlov * State Research Institute for Genetics and Selection of Industrial Microorganisms, Kurchatov Institute National Research Center (GosNIIgenetika, Kurchatov Institute NRC), Moscow, 117545 Russia *e-mail: dg_kozlov@genetika.ru Received July 9, 2018; revised December 18, 2018; accepted March 15, 2019 Abstract—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 eff iciency. At the same time, the bacterial enzyme, like eukaryotic DUBs, fails to process sites contain- ing 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. Keywords: ubiquitin, DUB, E. coli http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

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

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Publisher
Springer Journals
Copyright
Copyright © 2019 by Pleiades Publishing, Inc.
Subject
Life Sciences; Biochemistry, general; Microbiology; Medical Microbiology
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1134/S0003683819090060
Publisher site
See Article on Publisher Site

Abstract

ISSN 0003-6838, Applied Biochemistry and Microbiology, 2019, Vol. 55, No. 9, pp. 846–849. © Pleiades Publishing, Inc., 2019. Russian Text © The Author(s), 2019, published in Biotekhnologiya, 2019, Vol. 35, No. 2, pp. 25–29. PRODUCERS, BIOLOGY, SELECTION, AND GENE ENGINEERING Ubiquitin-Specif ic E. coli Proteinase Does Not Require the Obligatory Presence of Dipeptide GlyGly at Processing Site a a a, E. P. Sannikova , S. E. Cheperegin , and D. G. Kozlov * State Research Institute for Genetics and Selection of Industrial Microorganisms, Kurchatov Institute National Research Center (GosNIIgenetika, Kurchatov Institute NRC), Moscow, 117545 Russia *e-mail: dg_kozlov@genetika.ru Received July 9, 2018; revised December 18, 2018; accepted March 15, 2019 Abstract—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 eff iciency. At the same time, the bacterial enzyme, like eukaryotic DUBs, fails to process sites contain- ing 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. Keywords: ubiquitin, DUB, E. coli

Journal

Applied Biochemistry and Microbiology – Springer Journals

Published: Dec 5, 2019

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