ArticlemBio2016
Ubiquitin-Like Proteasome System Represents a Eukaryotic-Like Pathway for Targeted Proteolysis in Archaea.
Article in mBio, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- Review
- Oxidative Stress-Mediated RUNX3 Mislocalization Occurs Via Jun Activation Domain-Binding Protein 1 and Histone Modification.Applied biochemistry and biotechnology · 2024Article
- Degron-controlled protein degradation inbioRxiv : the preprint server for biology · 2023Article
- Article
- Insights into the Lysine Acetylome of the HaloarchaeonAntioxidants (Basel, Switzerland) · 2023Article
- Application of Archaea in Deubiquitinase-Like Enzyme Discovery and Activity Assay.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Live-cell fluorescence imaging of microgametogenesis in the human malaria parasite Plasmodium falciparum.PLoS pathogens · 2022Article
- Expression and tandem affinity purification of 20S proteasomes and other multisubunit complexes in Haloferax volcanii.Methods in enzymology · 2021Article
- The proteasome controls ESCRT-III-mediated cell division in an archaeon.Science (New York, N.Y.) · 2020Article
- Multidomain ribosomal protein trees and the planctobacterial origin of neomura (eukaryotes, archaebacteria).Protoplasma · 2020Review
- Gene Expression ofInternational journal of molecular sciences · 2019Article
- Rhodanese-Like Domain Protein UbaC and Its Role in Ubiquitin-Like Protein Modification and Sulfur Mobilization in Archaea.Journal of bacteriology · 2019Article
- Stepping up protein degradation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Assays for ubiquitin-like protein ligation and proteasome function in archaea.Methods in enzymology · 2019Article
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Molecular Factors of Hypochlorite Tolerance in the Hypersaline Archaeon Haloferax volcanii.Genes · 2018Article
- Rpn11-mediated ubiquitin processing in an ancestral archaeal ubiquitination system.Nature communications · 2018Article
- Multiplex quantitative SILAC for analysis of archaeal proteomes: a case study of oxidative stress responses.Environmental microbiology · 2018Article
- Methionine Sulfoxide Reductase A (MsrA) and Its Function in Ubiquitin-Like Protein Modification inmBio · 2017Article
- Mycobacterium tuberculosis proteasomal ATPase Mpa has a β-grasp domain that hinders docking with the proteasome core protease.Molecular microbiology · 2017Article
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 1 institution in 2 countries.
Funding
Abstract
unlabelledThe molecular mechanisms of targeted proteolysis in archaea are poorly understood, yet they may have deep evolutionary roots shared with the ubiquitin-proteasome system of eukaryotic cells. Here, we demonstrate in archaea that TBP2, a TATA-binding protein (TBP) modified by ubiquitin-like isopeptide bonds, is phosphorylated and targeted for degradation by proteasomes. Rapid turnover of TBP2 required the functions of UbaA (the E1/MoeB/ThiF homolog of archaea), AAA ATPases (Cdc48/p97 and Rpt types), a type 2 JAB1/MPN/MOV34 metalloenzyme (JAMM/MPN+) homolog (JAMM2), and 20S proteasomes. The ubiquitin-like protein modifier small archaeal modifier protein 2 (SAMP2) stimulated the degradation of TBP2, but SAMP2 itself was not degraded. Analysis of the TBP2 fractions that were not modified by ubiquitin-like linkages revealed that TBP2 had multiple N termini, including Met1-Ser2, Ser2, and Met1-Ser2(p) [where (p) represents phosphorylation]. The evidence suggested that the Met1-Ser2(p) form accumulated in cells that were unable to degrade TBP2. We propose a model in archaea in which the attachment of ubiquitin-like tags can target proteins for degradation by proteasomes and be controlled by N-terminal degrons. In support of a proteolytic mechanism that is energy dependent and recycles the ubiquitin-like protein tags, we find that a network of AAA ATPases and a JAMM/MPN+ metalloprotease are required, in addition to 20S proteasomes, for controlled intracellular proteolysis. IMPORTANCE: This study advances the fundamental knowledge of signal-guided proteolysis in archaea and sheds light on components that are related to the ubiquitin-proteasome system of eukaryotes. In archaea, the ubiquitin-like proteasome system is found to require function of an E1/MoeB/ThiF homolog, a type 2 JAMM/MPN+ metalloprotease, and a network of AAA ATPases for the targeted destruction of proteins. We provide evidence that the attachment of the ubiquitin-like protein is controlled by an N-terminal degron and stimulates proteasome-mediated proteolysis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.