Universität zu Köln

Jin, Bo, Wang, Jiayue, Liu, Xiangnan, Fang, Shuai, Jiang, Bo, Hofmann, Kay ORCID: 0000-0002-2289-9083, Yin, Jun and Zhao, Bo (2018). Ubiquitin-Mimicking Peptides Transfer Differentiates by E1 and E2 Enzymes. Biomed Res. Int., 2018. LONDON: HINDAWI LTD. ISSN 2314-6141

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Abstract

Ubiquitin and ubiquitin like proteins (UBLs) play key roles in eukaryotes. These proteins are attached to their target proteins through an E1-E2-E3 cascade and modify the functions of these proteins. Since the discovery of ubiquitin, several UBLs have been identified, including Nedd8, SUMO, ISG15, and Atg8. Ubiquitin and UBLs share a similar three-dimensional structure: beta=grasp fold and an X-X-[R/A/E/K]-X-X-[G/X]-G motif at the C-terminus. We have previously reported that ubiquitin, Nedd8, and SUMO mimicking peptides which all contain the conserved motif X-X-[R/A/E/K]-X-X-[G/X]-G still retained their reactivity toward their corresponding E1, E2, and E3 enzymes. In our current study, we investigated whether such C-terminal peptides could still be transferred onto related pathway enzymes to probe the function of these enzymes when they are fused with a protein. By bioinformatic search of protein databases, we selected eight proteins carrying the X-X-[R/A/E/K]-X-X-[G/X]-G motif at the C-terminus of the beta-grasp fold. We synthesized the C-terminal sequences of these candidates as short peptides and found that three of them showed significant reactivity with the ubiquitin E1 enzyme Ubel. We next fused the three reactive short peptides to three different protein frames, including their respective native protein frames, a ubiquitin frame and a peptidyl carrier protein (PCP) frame, and measured the reactivities of these peptide-fused proteins with Ubel. Peptide-fused proteins on ubiquitin and PCP frames showed obvious reactivity with Ubel. However, when we measured E2 UbcH7 transfer, we found that the PCP-peptide fusions lost their reactivity with UbcH7. Taken together, these results suggested that the recognition of E2 enzymes with peptide-fused proteins depended not only on the C-terminal sequences of the ubiquitin-mimicking peptides, but also on the overall structures of the protein frames.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Jin, Bo UNSPECIFIED UNSPECIFIED UNSPECIFIED Wang, Jiayue UNSPECIFIED UNSPECIFIED UNSPECIFIED Liu, Xiangnan UNSPECIFIED UNSPECIFIED UNSPECIFIED Fang, Shuai UNSPECIFIED UNSPECIFIED UNSPECIFIED Jiang, Bo UNSPECIFIED UNSPECIFIED UNSPECIFIED Hofmann, Kay UNSPECIFIED orcid.org/0000-0002-2289-9083 UNSPECIFIED Yin, Jun UNSPECIFIED UNSPECIFIED UNSPECIFIED Zhao, Bo UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-202058
DOI:	10.1155/2018/6062520
Journal or Publication Title:	Biomed Res. Int.
Volume:	2018
Date:	2018
Publisher:	HINDAWI LTD
Place of Publication:	LONDON
ISSN:	2314-6141
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Biology > Institute for Genetics
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language NEDD8; NEDDYLATION; ACTIVATION; EVOLUTION; CASCADE; SUMO Multiple languages Biotechnology & Applied Microbiology; Medicine, Research & Experimental Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/20205