Urmylation and tRNA thiolation functions of ubiquitin-like Uba4.Urm1 systems are conserved from yeast to man

Abstract

The ubiquitin‐like protein Urm1 from budding yeast and its E1‐like activator Uba4 have dual roles in protein urmylation and tRNA thiolation pathways. To study whether these are conserved among eukaryotes, we used gene shuffles to replace the yeast proteins by their human counterparts, hURM1 and hUBA4/MOCS3. As judged from biochemical and genetical assays, hURM1 and hUBA4 are functional in yeast, albeit at reduced efficiencies. They mediate urmylation of the peroxiredoxin Ahp1, a known urmylation target in yeast, and support tRNA thiolation. Similar to hUBA4, yeast Uba4 itself is modified by Urm1 and hURM1 suggesting target overlap between eukaryal urmylation pathways. In sum, our study shows that dual‐function ubiquitin‐like Urm1·Uba4 systems are conserved and exchangeable between human and yeast cells.

Autoren

André Jüdes
Folke Ebert
Christian Bär
Kathrin L Thüring
Aileen Harrer
Roland Klassen
Mark Helm
Michael JR Stark
Raffael Schaffrath

DOI

10.1016/j.febslet.2015.02.024

eISSN

1873-3468

ISSN

0014-5793

Ausgabe der Veröffentlichung

8

Zeitschrift

FEBS Letters

Sprache

en

Online publication date

2015

Paginierung

904 - 909

Datum der Veröffentlichung

2015

Status

Published

Herausgeber

Wiley

Herausgeber URL

http://dx.doi.org/10.1016/j.febslet.2015.02.024

Datum der Datenerfassung

2023

Titel

Urmylation and tRNA thiolation functions of ubiquitin‐like Uba4·Urm1 systems are conserved from yeast to man

Ausgabe der Zeitschrift

589

Datenquelle: Crossref

Abstract

The ubiquitin-like protein Urm1 from budding yeast and its E1-like activator Uba4 have dual roles in protein urmylation and tRNA thiolation pathways. To study whether these are conserved among eukaryotes, we used gene shuffles to replace the yeast proteins by their human counterparts, hURM1 and hUBA4/MOCS3. As judged from biochemical and genetical assays, hURM1 and hUBA4 are functional in yeast, albeit at reduced efficiencies. They mediate urmylation of the peroxiredoxin Ahp1, a known urmylation target in yeast, and support tRNA thiolation. Similar to hUBA4, yeast Uba4 itself is modified by Urm1 and hURM1 suggesting target overlap between eukaryal urmylation pathways. In sum, our study shows that dual-function ubiquitin-like Urm1·Uba4 systems are conserved and exchangeable between human and yeast cells.

Addresses

Universität Kassel, Institut für Biologie, FG Mikrobiologie, Heinrich-Plett-Str. 40, 34132 Kassel, Germany.

Autoren

André Jüdes
Folke Ebert
Christian Bär
Kathrin L Thüring
Aileen Harrer
Roland Klassen
Mark Helm
Michael JR Stark
Raffael Schaffrath

DOI

10.1016/j.febslet.2015.02.024

eISSN

1873-3468

Externe Identifier

PubMed Identifier: 25747390

Funding acknowledgements

Wellcome Trust: 097945

Open access

false

ISSN

0014-5793

Ausgabe der Veröffentlichung

8

Zeitschrift

FEBS letters

Schlüsselwörter

Hela Cells
Humans
Saccharomyces cerevisiae
Nucleotidyltransferases
Sulfurtransferases
Saccharomyces cerevisiae Proteins
Ubiquitins
RNA, Transfer
Anticodon
Conserved Sequence
Sequence Homology, Amino Acid

Sprache

eng

Medium

Print-Electronic

Online publication date

2015

Paginierung

904 - 909

Datum der Veröffentlichung

2015

Status

Published

Datum der Datenerfassung

2015

Titel

Urmylation and tRNA thiolation functions of ubiquitin-like Uba4·Urm1 systems are conserved from yeast to man.

Sub types

Research Support, Non-U.S. Gov't
Journal Article

Ausgabe der Zeitschrift

589

Datenquelle: Europe PubMed Central

Abstract

The ubiquitin-like protein Urm1 from budding yeast and its E1-like activator Uba4 have dual roles in protein urmylation and tRNA thiolation pathways. To study whether these are conserved among eukaryotes, we used gene shuffles to replace the yeast proteins by their human counterparts, hURM1 and hUBA4/MOCS3. As judged from biochemical and genetical assays, hURM1 and hUBA4 are functional in yeast, albeit at reduced efficiencies. They mediate urmylation of the peroxiredoxin Ahp1, a known urmylation target in yeast, and support tRNA thiolation. Similar to hUBA4, yeast Uba4 itself is modified by Urm1 and hURM1 suggesting target overlap between eukaryal urmylation pathways. In sum, our study shows that dual-function ubiquitin-like Urm1·Uba4 systems are conserved and exchangeable between human and yeast cells.

Date of acceptance

2015

Autoren

André Jüdes
Folke Ebert
Christian Bär
Kathrin L Thüring
Aileen Harrer
Roland Klassen
Mark Helm
Michael JR Stark
Raffael Schaffrath

Autoren-URL

https://www.ncbi.nlm.nih.gov/pubmed/25747390

DOI

10.1016/j.febslet.2015.02.024

eISSN

1873-3468

Funding acknowledgements

Wellcome Trust: 097945

Ausgabe der Veröffentlichung

8

Zeitschrift

FEBS Lett

Schlüsselwörter

Saccharomyces cerevisiae
Uba4 (hUBA4/MOCS3)
Ubiquitin-like urmylation
Urm1 (hURM1)
tRNA thiolation
Anticodon
Conserved Sequence
HeLa Cells
Humans
Nucleotidyltransferases
RNA, Transfer
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Sequence Homology, Amino Acid
Sulfurtransferases
Ubiquitins

Sprache

eng

Country

England

Paginierung

904 - 909

PII

S0014-5793(15)00116-7

Datum der Veröffentlichung

2015

Status

Published

Datum, an dem der Datensatz öffentlich gemacht wurde

2015

Titel

Urmylation and tRNA thiolation functions of ubiquitin-like Uba4·Urm1 systems are conserved from yeast to man.

Sub types

Journal Article
Research Support, Non-U.S. Gov't

Ausgabe der Zeitschrift

589

Datenquelle: PubMed

Urmylation and tRNA thiolation functions of ubiquitin-like Uba4.Urm1 systems are conserved from yeast to man

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