Rhodanese-Like Domain Protein UbaC and Its Role in Ubiquitin-Like Protein Modification and Sulfur Mobilization in Archaea
Abstract
Ubiquitin-like protein (Ubl) modification targets proteins for transient inactivation and/or proteasome-mediated degradation in archaea. In this work the rhodanese-like domain (RHD) protein UbaC was found to copurify with the E1-like enzyme (UbaA) of the Ubl modification machinery in the archaeonHaloferax volcanii. UbaC was shown to be important for Ubl ligation, particularly for the attachment of the Ubl SAMP2/3s to protein targets after exposure to oxidants (NaOCl, dimethyl sulfoxide [DMSO], and methionine sulfoxide [MetO]) and the proteasome inhibitor bortezomib. While UbaC was needed for ligation of the Ubl SAMP1 to MoaE (the large subunit of molybdopterin synthase), it was not important in the formation of oxidant-induced SAMP1 protein conjugates. Indicative of defects in sulfur relay, mutation ofubaCimpaired molybdenum cofactor (Moco)-dependent DMSO reductase activity and cell survival at elevated temperature, suggesting a correlation with defects in the 2-thiolated state of wobble uridine tRNA. Overall, the archaeal stand-alone RHD UbaC has an important function in Ubl ligation and is associated with sulfur relay processes.
- Authors:
-
- Univ. of Florida, Gainesville, FL (United States)
- Publication Date:
- Research Org.:
- Univ. of Florida, Gainesville, FL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences, and Biosciences Division; National Institutes of Health (NIH)
- OSTI Identifier:
- 1609593
- Grant/Contract Number:
- FG02-05ER15650
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Journal of Bacteriology
- Additional Journal Information:
- Journal Volume: 201; Journal Issue: 15; Journal ID: ISSN 0021-9193
- Publisher:
- American Society for Microbiology
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; microbiology; rhodanese-like domain; post-translational modification; molybdopterin biosynthesis; 22 sulfur relay; tRNA thiolation; ubiquitin; proteasomes; archaea
Citation Formats
Hepowit, Nathaniel L., and Maupin-Furlow, Julie A. Rhodanese-Like Domain Protein UbaC and Its Role in Ubiquitin-Like Protein Modification and Sulfur Mobilization in Archaea. United States: N. p., 2019.
Web. doi:10.1128/jb.00254-19.
Hepowit, Nathaniel L., & Maupin-Furlow, Julie A. Rhodanese-Like Domain Protein UbaC and Its Role in Ubiquitin-Like Protein Modification and Sulfur Mobilization in Archaea. United States. https://doi.org/10.1128/jb.00254-19
Hepowit, Nathaniel L., and Maupin-Furlow, Julie A. Wed .
"Rhodanese-Like Domain Protein UbaC and Its Role in Ubiquitin-Like Protein Modification and Sulfur Mobilization in Archaea". United States. https://doi.org/10.1128/jb.00254-19. https://www.osti.gov/servlets/purl/1609593.
@article{osti_1609593,
title = {Rhodanese-Like Domain Protein UbaC and Its Role in Ubiquitin-Like Protein Modification and Sulfur Mobilization in Archaea},
author = {Hepowit, Nathaniel L. and Maupin-Furlow, Julie A.},
abstractNote = {Ubiquitin-like protein (Ubl) modification targets proteins for transient inactivation and/or proteasome-mediated degradation in archaea. In this work the rhodanese-like domain (RHD) protein UbaC was found to copurify with the E1-like enzyme (UbaA) of the Ubl modification machinery in the archaeonHaloferax volcanii. UbaC was shown to be important for Ubl ligation, particularly for the attachment of the Ubl SAMP2/3s to protein targets after exposure to oxidants (NaOCl, dimethyl sulfoxide [DMSO], and methionine sulfoxide [MetO]) and the proteasome inhibitor bortezomib. While UbaC was needed for ligation of the Ubl SAMP1 to MoaE (the large subunit of molybdopterin synthase), it was not important in the formation of oxidant-induced SAMP1 protein conjugates. Indicative of defects in sulfur relay, mutation ofubaCimpaired molybdenum cofactor (Moco)-dependent DMSO reductase activity and cell survival at elevated temperature, suggesting a correlation with defects in the 2-thiolated state of wobble uridine tRNA. Overall, the archaeal stand-alone RHD UbaC has an important function in Ubl ligation and is associated with sulfur relay processes.},
doi = {10.1128/jb.00254-19},
journal = {Journal of Bacteriology},
number = 15,
volume = 201,
place = {United States},
year = {2019},
month = {7}
}
Web of Science
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