ArticleJournal of bacteriology2004
Differential regulation of the PanA and PanB proteasome-activating nucleotidase and 20S proteasomal proteins of the haloarchaeon Haloferax volcanii.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 57 citations in OpenAlex.
- CdrS Is a Global Transcriptional Regulator Influencing Cell Division in Haloferax volcanii.mBio · 2021Article
- The Role of Stress Proteins in Haloarchaea and Their Adaptive Response to Environmental Shifts.Biomolecules · 2020Review
- 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
- Conformational switching in the coiled-coil domains of a proteasomal ATPase regulates substrate processing.Nature communications · 2018Article
- Article
- Structural and biochemical properties of an extreme 'salt-loving' proteasome activating nucleotidase from the archaeon Haloferax volcanii.Extremophiles : life under extreme conditions · 2014Article
- Article
- Ionic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP1) from Haloferax volcanii.Protein science : a publication of the Protein Society · 2013Article
- Post-translation modification in Archaea: lessons from Haloferax volcanii and other haloarchaea.FEMS microbiology reviews · 2013Review
- Prokaryotic proteasomes: nanocompartments of degradation.Journal of molecular microbiology and biotechnology · 2013Review
- Archaeal proteasomes and sampylation.Sub-cellular biochemistry · 2013Review
- AglS, a novel component of the Haloferax volcanii N-glycosylation pathway, is a dolichol phosphate-mannose mannosyltransferase.Journal of bacteriology · 2012Article
- The archaeal proteasome is regulated by a network of AAA ATPases.The Journal of biological chemistry · 2012Article
- Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid.Molecular microbiology · 2012Article
- Stress regulation of the PAN-proteasome system in the extreme halophilic archaeon Halobacterium.Extremophiles : life under extreme conditions · 2012Article
- Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Proteasomes and protein conjugation across domains of life.Nature reviews. Microbiology · 2011Review
- Phosphorylation and methylation of proteasomal proteins of the haloarcheon Haloferax volcanii.Archaea (Vancouver, B.C.) · 2010Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The halophilic archaeon Haloferax volcanii produces three different proteins (alpha1, alpha2, and beta) that assemble into at least two 20S proteasome isoforms. This work reports the cloning and sequencing of two H. volcanii proteasome-activating nucleotidase (PAN) genes (panA and panB). The deduced PAN proteins were 60% identical with Walker A and B motifs and a second region of homology typical of AAA ATPases. The most significant region of divergence was the N terminus predicted to adopt a coiled-coil conformation involved in substrate recognition. Of the five proteasomal proteins, the alpha1, beta, and PanA proteins were the most abundant. Differential regulation of all five genes was observed, with a four- to eightfold increase in mRNA levels as cells entered stationary phase. In parallel with this mRNA increase, the protein levels of PanB and alpha2 increased severalfold during the transition from exponential growth to stationary phase, suggesting that these protein levels are regulated at least in part by mechanisms that control transcript levels. In contrast, the beta and PanA protein levels remained relatively constant, while the alpha1 protein levels exhibited only a modest increase. This lack of correlation between the mRNA and protein levels for alpha1, beta, and PanA suggests posttranscriptional mechanisms are involved in regulating the levels of these major proteasomal proteins. Together these results support a model in which the cell regulates the ratio of the different 20S proteasome and PAN proteins to modulate the structure and ultimately the function of this central energy-dependent proteolytic system.
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