A proteomics approach to identify targets of the ubiquitin-like molecule Urm1 in Drosophila melanogaster.

ABSTRACT: By covalently conjugating to target proteins, ubiquitin-like modifiers (UBLs) act as important regulators of target protein localization and activity, thereby playing a critical role in the orchestration of cellular biology. The most ancient and one of the least studied UBLs is Urm1, a dual-function protein that in parallel to performing similar functions as its prokaryotic ancestors in tRNA modification, also has adopted the capacity to conjugate to cellular proteins analogous to ubiquitin and other UBL modifiers. In order to increase the understanding of Urm1 and its role in multicellular organisms, we have used affinity purification followed by mass spectrometry to identify putative targets of Urm1 conjugation (urmylation) at three developmental stages of the Drosophila melanogaster lif

SUBMITTER: Khoshnood B 

PROVIDER: S-EPMC5617222 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature