Literature DB >> 33291646

Proteasome Biology: Chemistry and Bioengineering Insights.

Lucia Račková1, Erika Csekes1.   

Abstract

Proteasomal degradation provides the crucial machinery for maintaining cellular proteostasis. The biological origins of modulation or impairment of the function of proteasomal complexes may include changes in gene expression of their subunits, ubiquitin mutation, or indirect mechanisms arising from the overall impairment of proteostasis. However, changes in the physico-chemical characteristics of the cellular environment might also meaningfully contribute to altered performance. This review summarizes the effects of physicochemical factors in the cell, such as pH, temperature fluctuations, and reactions with the products of oxidative metabolism, on the function of the proteasome. Furthermore, evidence of the direct interaction of proteasomal complexes with protein aggregates is compared against the knowledge obtained from immobilization biotechnologies. In this regard, factors such as the structures of the natural polymeric scaffolds in the cells, their content of reactive groups or the sequestration of metal ions, and processes at the interface, are discussed here with regard to their influences on proteasomal function.

Entities:  

Keywords:  immobilization; posttranslational modifications; proteasome; protein aggregates

Year:  2020        PMID: 33291646      PMCID: PMC7761984          DOI: 10.3390/polym12122909

Source DB:  PubMed          Journal:  Polymers (Basel)        ISSN: 2073-4360            Impact factor:   4.329


  310 in total

1.  A gated channel into the proteasome core particle.

Authors:  M Groll; M Bajorek; A Köhler; L Moroder; D M Rubin; R Huber; M H Glickman; D Finley
Journal:  Nat Struct Biol       Date:  2000-11

Review 2.  Protein chemical modification on endogenous amino acids.

Authors:  Emmanuel Baslé; Nicolas Joubert; Mathieu Pucheault
Journal:  Chem Biol       Date:  2010-03-26

Review 3.  Protein aggregation from inclusion bodies to amyloid and biomaterials.

Authors:  Anna Mitraki
Journal:  Adv Protein Chem Struct Biol       Date:  2010       Impact factor: 3.507

Review 4.  Oxidative stress-mediated regulation of proteasome complexes.

Authors:  Charity T Aiken; Robyn M Kaake; Xiaorong Wang; Lan Huang
Journal:  Mol Cell Proteomics       Date:  2011-05       Impact factor: 5.911

5.  Peroxynitrite-induced oxidation and its effects on isolated proteasomal systems.

Authors:  Manila Amici; Giulio Lupidi; Mauro Angeletti; Evandro Fioretti; Anna Maria Eleuteri
Journal:  Free Radic Biol Med       Date:  2003-04-15       Impact factor: 7.376

Review 6.  4-Hydroxynonenal (HNE) modified proteins in metabolic diseases.

Authors:  José Pedro Castro; Tobias Jung; Tilman Grune; Werner Siems
Journal:  Free Radic Biol Med       Date:  2016-11-01       Impact factor: 7.376

7.  Identification of bovine heart cytochrome c oxidase subunits modified by the lipid peroxidation product 4-hydroxy-2-nonenal.

Authors:  Andrej Musatov; Christopher A Carroll; Yuan-Chao Liu; George I Henderson; Susan T Weintraub; Neal C Robinson
Journal:  Biochemistry       Date:  2002-06-25       Impact factor: 3.162

8.  Tyrosine nitration of PA700 links proteasome activation to endothelial dysfunction in mouse models with cardiovascular risk factors.

Authors:  Jian Xu; Shuangxi Wang; Miao Zhang; Qilong Wang; Sima Asfa; Ming-Hui Zou
Journal:  PLoS One       Date:  2012-01-17       Impact factor: 3.240

Review 9.  PA28αβ: the enigmatic magic ring of the proteasome?

Authors:  Paolo Cascio
Journal:  Biomolecules       Date:  2014-06-19

Review 10.  Fundamentals on the biochemistry of peroxynitrite and protein tyrosine nitration.

Authors:  Silvina Bartesaghi; Rafael Radi
Journal:  Redox Biol       Date:  2017-09-19       Impact factor: 11.799

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