Recombinant ATPases of the yeast 26S proteasome activate protein degradation by the 20S proteasome

TAKEUCHI, J

doi:10.1016/s0014-5793(04)00378-3

Cited by 3 publications

(3 citation statements)

References 18 publications

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“…To explore more about the general applicability of FATT‐fusion as a way to facilitate soluble expression, six base subunits from the 19S proteasomal complex were individually expressed as either FATT‐ or GST‐fusion proteins. Bacterial expression of these proteins (Rpt1–6) has been very difficult because the individual subunits have a strong tendency to aggregate, and even the solubility‐enhancing GST‐tag showed very limited effects [Fig. (B), panels "GST"].…”

Section: Resultsmentioning

confidence: 99%

A multipurpose fusion tag derived from an unstructured and hyperacidic region of the amyloid precursor protein

et al. 2013

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Expression and purification of aggregation-prone and disulfide-containing proteins in Escherichia coli remains as a major hurdle for structural and functional analyses of high-value target proteins. Here, we present a novel gene-fusion strategy that greatly simplifies purification and refolding procedure at very low cost using a unique hyperacidic module derived from the human amyloid precursor protein. Fusion with this polypeptide (dubbed FATT for Flag-Acidic-Target Tag) results in near-complete soluble expression of variety of extracellular proteins, which can be directly refolded in the crude bacterial lysate and purified in one-step by anion exchange chromatography. Application of this system enabled preparation of functionally active extracellular enzymes and antibody fragments without the need for condition optimization.

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Section: Resultsmentioning

confidence: 99%

A multipurpose fusion tag derived from an unstructured and hyperacidic region of the amyloid precursor protein

et al. 2013

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“…Therefore, it could be suggested that 20S proteasome first binds with base, which is followed by attachment of lid complex. The ATPases are also required for the assembly of 19S proteasome, since yeast ATPases genes co‐expression in E. coli is able to provide a heterohexameric complex present in the base of 19S . On the basis of mass spectrometry analysis of yeast lid complex, two clusters of 19S assembly intermediates have been identified: first one is composed of Rpn5, 6, 8, 9, 11 and the other one is of Rpn3, 7, 12, and 15, in which interaction between Rpn3 and 5 joins both the clusters .…”

Section: Understanding and Synchronization Of The Organization Of A Cmentioning

confidence: 99%

Proteasome‐mediated proteostasis: Novel medicinal and pharmacological strategies for diseases

Mishra

Upadhyay

Prajapati

et al. 2018

Medicinal Research Reviews

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Proteins actively participate in a wide range of cellular physiological functions. But aggregation of proteins results in cytotoxicity, and unwanted aggregation of misfolded proteins often causes many diseases. During abnormal protein aggregation events, cells try to cope against such deleterious consequences because of the remarkable functional attempts of two distinct proteolytic mechanisms. These tightly regulative and signaling mechanisms are autophagy pathway and ubiquitin proteasome system. Proteasome complex system holds the elimination capacity of intracellular aberrant protein aggregation. Despite the considerable progress that has been achieved, which elucidates wide function and diverse roles of proteasome system, still several crucial problems remain unanswered. For example, how the complex proteasomes assembly and their interactive pathways determine the precise sense of several proteotoxic insults, which can severely affect the cell survival and homeostasis? The specific degradation of various aberrant proteins that can disturb cellular homeostasis is achieved by proper proteasome functionality, which is yet another unclear and critical challenge. Therefore, a better understanding of the various cellular signaling mechanisms composing the proteasome machinery carries broad therapeutic implications linked with proteopathies. This article signifies the urgent need, which is now crucial for us to improve our understanding of the proteasome architecture, structure, and functions that span multiple level strategies from the molecular level to the cellular level. This systematic in-depth information of proteasome may be helpful in the near future to design a new molecular framework based on intrinsic and extrinsic cellular mechanisms that drive the assembly of proteasome to induce cellular survival against proteostasis imbalance and disease conditions.

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“…The main eukaryotic degradation machinery, the 26S proteasome, specifically degrades ubiquitinylated proteins (Miller and Gordon, 2005). Proteolysis is performed by the ATPindependent peptidase activity of the 20S core of the proteasome, whereas substrate specificity is mediated by the 19S regulatory particle consisting of a base complex which confers ATPase and chaperon activity and a 26S lid complex of so far unknown function (Takeuchi and Tamura, 2004). Proteins are targeted for degradation by poly-conjugation of the small ubiquitin protein.…”

Section: Introductionmentioning

confidence: 99%

CsnA Dependent Development and Regulation of Amino Acid Biosynthesis of the Filamentous Ascomycete <i>Aspergillus nidulans</i>

Oliver¹

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Chapter 1were found: the ones that exhibit light-grown seedling characteristics in the absence of light, a constitutive photomorphogenesis (cop) and the other group of mutants that showed deethiolation (det) . Lethal mutants in this class are allelic to fusca mutants which accumulate anthocyanin, a purple pigment, in the mature seed coat and the embryonic leaves (Gusmaroli et al., 2004;Misera et al., 1994). These mutants were classed as cop/det/fus mutants in A. thaliana and later on it could be shown that their respective gene loci coded for six of the eight subunits of the COP9 signalosome Wei et al., 1998). The mammalian CSN complex is also known as the JAB containing signalosome according to the fifth subunit JAB1 (Carrabino et al., 2004). It was originally the N-terminal HAM domain. The WH-domain is a globular / s t r u c t u r e w i t h a n ""-arrangement, which can be classified as a winged-helix (WH) motif. The HAM domain is entirely helical with a core of six regularly-spaced helices that form three antiparallel helical hairpins. It resembles structurally mainly HEAT and Armadillo-repeats, creating the name HAM-domain. Scheel and Hofmann found that TPR-like (tetratrico-peptide repeats) repeats precede many PCI domains, which consist of short bi-helical segments.

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Recombinant ATPases of the yeast 26S proteasome activate protein degradation by the 20S proteasome

Cited by 3 publications

References 18 publications

A multipurpose fusion tag derived from an unstructured and hyperacidic region of the amyloid precursor protein

A multipurpose fusion tag derived from an unstructured and hyperacidic region of the amyloid precursor protein

Proteasome‐mediated proteostasis: Novel medicinal and pharmacological strategies for diseases

CsnA Dependent Development and Regulation of Amino Acid Biosynthesis of the Filamentous Ascomycete <i>Aspergillus nidulans</i>

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