Ubiquitination Accomplished: E1 and E2 Enzymes Were Not Necessary

Mark A Nakasone; Danny T Huang

doi:10.1016/j.molcel.2016.06.001

Ubiquitination Accomplished: E1 and E2 Enzymes Were Not Necessary

Mark A Nakasone
, Danny T Huang (Lead / Corresponding author)

Biological Chemistry and Drug Discovery

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

Abstract

Qiu et al. (2016) show that a mono-ADP-ribosyltransferase, SdeA, from Legionella pneumophila catalyzes ADP-ribosylation of ubiquitin, allowing SdeA to modify substrate with ubiquitin in the absence of E1 and E2 enzymes.

Original language	English
Pages (from-to)	807-809
Number of pages	3
Journal	Molecular Cell
Volume	62
Issue number	6
Early online date	16 Jun 2016
DOIs	https://doi.org/10.1016/j.molcel.2016.06.001
Publication status	Published - 16 Jun 2016

Keywords

ADP Ribose Transferases
Humans
Legionella pneumophila/enzymology
Ubiquitin
Ubiquitin-Conjugating Enzymes/genetics
Ubiquitination

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10.1016/j.molcel.2016.06.001

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title = "Ubiquitination Accomplished: E1 and E2 Enzymes Were Not Necessary",

abstract = "Qiu et al. (2016) show that a mono-ADP-ribosyltransferase, SdeA, from Legionella pneumophila catalyzes ADP-ribosylation of ubiquitin, allowing SdeA to modify substrate with ubiquitin in the absence of E1 and E2 enzymes.",

keywords = "ADP Ribose Transferases, Humans, Legionella pneumophila/enzymology, Ubiquitin, Ubiquitin-Conjugating Enzymes/genetics, Ubiquitination",

author = "Nakasone, \{Mark A\} and Huang, \{Danny T\}",

year = "2016",

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doi = "10.1016/j.molcel.2016.06.001",

language = "English",

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journal = "Molecular Cell",

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T2 - E1 and E2 Enzymes Were Not Necessary

AU - Nakasone, Mark A

AU - Huang, Danny T

PY - 2016/6/16

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N2 - Qiu et al. (2016) show that a mono-ADP-ribosyltransferase, SdeA, from Legionella pneumophila catalyzes ADP-ribosylation of ubiquitin, allowing SdeA to modify substrate with ubiquitin in the absence of E1 and E2 enzymes.

AB - Qiu et al. (2016) show that a mono-ADP-ribosyltransferase, SdeA, from Legionella pneumophila catalyzes ADP-ribosylation of ubiquitin, allowing SdeA to modify substrate with ubiquitin in the absence of E1 and E2 enzymes.

KW - ADP Ribose Transferases

KW - Humans

KW - Legionella pneumophila/enzymology

KW - Ubiquitin

KW - Ubiquitin-Conjugating Enzymes/genetics

KW - Ubiquitination

U2 - 10.1016/j.molcel.2016.06.001

DO - 10.1016/j.molcel.2016.06.001

M3 - Article

C2 - 27315555

SN - 1097-2765

VL - 62

SP - 807

EP - 809

JO - Molecular Cell

JF - Molecular Cell

IS - 6

ER -

Ubiquitination Accomplished: E1 and E2 Enzymes Were Not Necessary

Abstract

Keywords

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