ArticleProteomics2012
Chemical cross-linking, mass spectrometry, and in silico modeling of proteasomal 20S core particles of the haloarchaeon Haloferax volcanii.
Article in Proteomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026Review
- Review
- Expression and tandem affinity purification of 20S proteasomes and other multisubunit complexes in Haloferax volcanii.Methods in enzymology · 2021Article
- Assays for ubiquitin-like protein ligation and proteasome function in archaea.Methods in enzymology · 2019Article
- Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Post-translation modification in Archaea: lessons from Haloferax volcanii and other haloarchaea.FEMS microbiology reviews · 2013Review
- In vivo protein interaction network identified with a novel real-time cross-linked peptide identification strategy.Journal of proteome research · 2013Article
- XLink-DB: database and software tools for storing and visualizing protein interaction topology data.Journal of proteome research · 2013Article
- Large Scale Chemical Cross-linking Mass Spectrometry Perspectives.Journal of proteomics & bioinformatics · 2013Article
- Prokaryotic proteasomes: nanocompartments of degradation.Journal of molecular microbiology and biotechnology · 2013Review
- Archaeal proteasomes and sampylation.Sub-cellular biochemistry · 2013Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
A fast and accurate method is reported to generate distance constraints between juxtaposited amino acids and to validate molecular models of halophilic protein complexes. Proteasomal 20S core particles (CPs) from the haloarchaeon Haloferax volcanii were used to investigate the quaternary structure of halophilic proteins based on their symmetrical, yet distinct subunit composition. Proteasomal CPs are cylindrical barrel-like structures of four-stacked homoheptameric rings of α- and β-type subunits organized in α(7)β(7) β(7)α(7) stoichiometry. The CPs of H. volcanii are formed from a single type of β subunit associated with α1 and/or α2 subunits. Tandem affinity chromatography and new genetic constructs were used to separately isolate α1(7)β(7)β(7)α1(7) and α2(7)β(7)β(7)α2(7) CPs from H. volcanii. Chemically cross-linked peptides of the H. volcanii CPs were analyzed by high-performance mass spectrometry and an open modification search strategy to first generate and then to interpret the resulting tandem mass spectrometric data. Distance constraints obtained by chemical cross-linking mass spectrometry, together with the available structural data of nonhalophilic CPs, facilitated the selection of accurate models of H. volcanii proteasomal CPs composed of α1-, α2-, and β-homoheptameric rings from several different possible structures from Protein Data Bank.
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