Stress Response in Archaea

Macario, Alberto J. L.; Macario, Everly Conway de

doi:10.1002/0471263397.env318

Cited by 24 publications

(31 citation statements)

References 69 publications

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“…Hsps are an evolutionary conserved family of functionally related proteins, and many of them are molecular chaperones (Ellis, 1990;Ritossa, 1996;Walter and Buchner, 2002;Macario et al, 1999;Young et al, 2004). These are capable of recognizing and binding substrate proteins in an unstable or inactive state and assisting them in folding or refolding to achieve a native conformation.…”

Section: Discussionmentioning

confidence: 99%

“…Hsp60, a Group I chaperonin, is found in bacteria and eukaryotic organelles, whereas Group II chaperonins occur in Archea and eukaryotic cytosol, typically forming double-ringed structures (Macario et al, 1999;. At least nine genes have been identified for Group II but only one for Group I proteins in humans (Kubota et al, 1995;Hansen et al, 2003).…”

confidence: 99%

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Upon oxidative stress, the antiapoptotic Hsp60/procaspase-3 complex persists in mucoepidermoid carcinoma cells

Campanella¹,

Bucchieri²,

Ardizzone³

et al. 2009

Eur J Histochem

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Hsp60, a mitochondrial chaperonin highly conserved during evolution, has been found elevated in the cytosol of cancer cells, both in vivo and in vitro, but its role in determining apoptosis during oxidative stress (OS) has not yet been fully elucidated. The aim of the present work was to study the effects of OS on Hsp60 levels and its interactions with procaspase- 3 (p-C3) and p53 in tumor cells. NCI-H292 (mucoepidermoid carcinoma) cells were exposed to various concentrations of hydrogen peroxide (H2O2) for 24 hours. Cell viability was determined by Trypan blue and MTT assays. DNA damage was assessed by the Comet assay, and apoptosis was measured by the AnnexinV cytofluorimetric test. Exposure to increasing concentrations of H2O2 resulted in a reduction of cell viability, DNA damage, and early apoptotic phenomena. Hsp60, p-C3, p53, and p21 were assessed by Western blotting and immunocytochemistry before and after OS. Hsp60 and p-C3 were present before and after OS induction. Immunoprecipitation experiments showed an Hsp60/p-C3 complex before OS that persisted after it, while an Hsp60/p53 complex was not detected in either condition. The presence of wild type (wt) p53 was confirmed by RT-PCR, and p21 detection suggested p53 activation after OS. We postulate that, although OS may induce early apoptosis in NCI-H292 cells, Hsp60 exerts an anti-apoptotic effect in these cells and, by extension, it may do so in other cancer cells

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Section: Discussionmentioning

confidence: 99%

Upon oxidative stress, the antiapoptotic Hsp60/procaspase-3 complex persists in mucoepidermoid carcinoma cells

Campanella¹,

Bucchieri²,

Ardizzone³

et al. 2009

Eur J Histochem

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“…Genome sequencing projects on different methanosarcina, Methanosarcina mazei (Deppenmeier et al 2002), Methanosarcina acetivorans (Galagan et al 2002), and Methanosarcina barkeri (Maeder et al 2006), revealed that about 20-33 % of methanosarcina genes (∼1000 genes) have been acquired horizontally, including the genes encoding group I chaperonins from bacteria. These studies therefore presented the first evidence of the co-existence of group I (GroES/L) and group II (thermosome/prefoldin) chaperonin genes (Macario et al 1999(Macario et al , 2004) that are expressed concurrently (Klunker et al 2003), and distinct substrate pools (Hirtreiter et al 2009), thereby offering a fantastic model to study the evolution of chaperonin dependent protein folding. While the group II chaperonin genes that are exclusive to archaea and eukaryotes are understood to be inherited, group I chaperonin genes that are exclusive of bacterial cytosol and endosymbiotic organelle are believed to be acquired horizontally, indicating probable relationship between archaea and bacteria.…”

Section: Multiple Chaperonins In Rhizobium-the Division Of Labor Situmentioning

confidence: 99%

Multiple chaperonins in bacteria—novel functions and non-canonical behaviors

Kumar

Mande

Mahajan

2015

Cell Stress and Chaperones

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Chaperonins are a class of molecular chaperones that assemble into a large double ring architecture with each ring constituting seven to nine subunits and enclosing a cavity for substrate encapsulation. The well-studied Escherichia coli chaperonin GroEL binds non-native substrates and encapsulates them in the cavity thereby sequestering the substrates from unfavorable conditions and allowing the substrates to fold. Using this mechanism, GroEL assists folding of about 10-15 % of cellular proteins. Surprisingly, about 30 % of the bacteria express multiple chaperonin genes. The presence of multiple chaperonins raises questions on whether they increase general chaperoning ability in the cell or have developed specific novel cellular roles. Although the latter view is widely supported, evidence for the former is beginning to appear. Some of these chaperonins can functionally replace GroEL in E. coli and are generally indispensable, while others are ineffective and likewise are dispensable. Additionally, moonlighting functions for several chaperonins have been demonstrated, indicating a functional diversity among the chaperonins. Furthermore, proteomic studies have identified diverse substrate pools for multiple chaperonins. We review the current perception on multiple chaperonins and their physiological and functional specificities.

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“…3). In archaea, the protein chaperone systems are thought to utilize DnaK, prefoldin and the thermosome to bind unfolded proteins and mediate their folding (Macario et al, 1999). The DNA repair enzymes more highly expressed in response to copper were RecA/RadA and endonuclease IV (spots 12 and 17, respectively; Table 3).…”

Section: Growth Of Fer1 In the Presence Of Cu 2+mentioning

confidence: 99%

Molecular insight into extreme copper resistance in the extremophilic archaeon ‘Ferroplasma acidarmanus’ Fer1

et al. 2005

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‘Ferroplasma acidarmanus’ strain Fer1 is an extremely acidophilic archaeon involved in the genesis of acid mine drainage, and was isolated from copper-contaminated mine solutions at Iron Mountain, CA, USA. Here, the initial proteomic and molecular investigation of Cu2+ resistance in this archaeon is presented. Analysis of Cu2+ toxicity via batch growth experiments and inhibition of oxygen uptake in the presence of ferrous iron demonstrated that Fer1 can grow and respire in the presence of 20 g Cu2+ l−1. The Fer1 copper resistance (cop) loci [originally detected by Ettema, T. J. G., Huynen, M. A., de Vos, W. M. & van der Oost, J. Trends Biochem Sci 28, 170–173 (2003)] include genes encoding a putative transcriptional regulator (copY), a putative metal-binding chaperone (copZ) and a putative copper-transporting P-type ATPase (copB). Transcription analyses demonstrated that copZ and copB are co-transcribed, and transcript levels were increased significantly in response to exposure to high levels of Cu2+, suggesting that the transport system is operating for copper efflux. Proteomic analysis of Fer1 cells exposed to Cu2+ revealed the induction of stress proteins associated with protein folding and DNA repair (including RadA, thermosome and DnaK homologues), suggesting that ‘Ferroplasma acidarmanus’ Fer1 uses multiple mechanisms for resistance to high levels of copper.

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Stress Response in Archaea

Abstract: Terminology The Three Domains of Life The Beginnings Gene Cloning Discontinuous Distribution of the hsp70(dnaK) Gene within the Domain Archaea Stress Proteins in Archaea … Show more

Cited by 24 publications

References 69 publications

Upon oxidative stress, the antiapoptotic Hsp60/procaspase-3 complex persists in mucoepidermoid carcinoma cells

Upon oxidative stress, the antiapoptotic Hsp60/procaspase-3 complex persists in mucoepidermoid carcinoma cells

Multiple chaperonins in bacteria—novel functions and non-canonical behaviors

Molecular insight into extreme copper resistance in the extremophilic archaeon ‘Ferroplasma acidarmanus’ Fer1

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