Structure and function of Hsp78, the mitochondrial ClpB homolog

Leidhold, Claudia; Janowsky, Birgit von; Becker, Dorothea; Bender, Tom; Voos, Wolfgang

doi:10.1016/j.jsb.2006.04.007

Cited by 25 publications

(21 citation statements)

References 45 publications

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“…The molecular chaperone Hsp78, which confers compartment-specific thermo tolerance to mitochondria, is crucial for maintenance of respiratory competence and for mitochondrial genome integrity under severe temperature stress [28]. The hsp78 levels increased in a linear fashion and correlated with water temperatures in white muscle of rainbow trout ( Oncorhynchus mykiss ) [29] and in green sturgeon, Acipenser medirostris larvae, on continuous exposure to 26°C [30].…”

Section: Discussionmentioning

confidence: 99%

InvestigatinghspGene Expression in Liver ofChanna striatusunder Heat Stress for Understanding the Upper Thermal Acclimation

Purohit

Mahanty

Suar

et al. 2014

BioMed Research International

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Changes in hsp gene expression profiles in murrel Channa striatus experimentally exposed to temperature stress (36°C) for 4, 15, and 30 days were investigated; fish collected from aquaculture ponds and maintained in laboratory at the pond temperature (25 ± 1°C) served as control. Channa collected from a hot spring runoff (36°C) was included in the study to examine the hsp profiles beyond 30 days of exposure. Gene expression analyses of a battery of hsps in liver tissues were carried out by quantitative RT-PCR and protein expressions were analyzed by immunoblotting. hsps could be grouped into three clusters based on similarity in response to heat stress: hsp70, hsp78, and hsp60, whose transcript level continued to increase with duration of exposure; hsp90 and hsp110 that increased to a much higher level and then decreased; hsp27 and hsp47 that did not significantly vary as compared to control. The results suggest that Hsp70, Hsp78, and Hsp60 are involved in thermal acclimation and long term survival at high temperature. Fish living in the hot spring runoff appears to continuously express hsps that can be approximated by long term induction of hsps in farmed fish if temperature of their environment is raised to 36°C.

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Section: Discussionmentioning

confidence: 99%

InvestigatinghspGene Expression in Liver ofChanna striatusunder Heat Stress for Understanding the Upper Thermal Acclimation

Purohit

Mahanty

Suar

et al. 2014

BioMed Research International

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“…The disaggregases ClpBand ClpC [98, 101, 102] in bacteria, Hsp104 and Hsp78 [103–106] in yeast, as well as Hsp101 [107–110] in plants, all contain a coiled-coil insertion toward the C-terminal end of NBD1. ClpE is another bacterial homologue that contains a coiled-coil insertion[111, 112].…”

Section: The Function Of the MDmentioning

confidence: 99%

The elusive middle domain of Hsp104 and ClpB: Location and function

DeSantis

Shorter

2012

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Hsp104 in yeast and ClpB in bacteria are homologous, hexameric AAA+ proteins and Hsp100 chaperones that function in the stress response as ring-translocases that drive protein disaggregation and reactivation. Both Hsp104 and ClpB contain a distinctive coiled-coil middle domain (MD) inserted in the first AAA+ domain, which distinguishes them from other AAA+ proteins and Hsp100 family members. Here, we focus on recent developments concerning the location and function of the MD in these hexameric molecular machines, which remains an outstanding question. While the atomic structure of the hexameric assembly of Hsp104 and ClpB remains uncertain, recent advances have illuminated that the MD is critical for the intrinsic disaggregase activity of the hexamer and mediates key functional interactions with the Hsp70 chaperone system (Hsp70 and Hsp40) that empower protein disaggregation.

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“…Although induced thermotolerance of the yeast strain lacking Hsp104 is severely impaired, it is not completely abolished, suggesting that other heat shock stimulated factors may also contribute to this phenomenon [11]. While Hsp104 is conserved in prokaryotes (where it is called ClpB), fungi and plants, as well as in animal mitochondria, its cytoplasmic orthologs were not found in multicellular animals thus far (for review, see [21]). Nevertheless, the phenomenon of induced thermotolerance is detected in animal cells, indicating that other animal proteins may serve as functional analogs of Hsp104.…”

Section: General Characterization Of Hsp104mentioning

confidence: 99%

Hsp104 and Prion Propagation

Romanova

Chernoff

2009

PPL

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High-ordered aggregates (amyloids) may disrupt cell functions, cause toxicity at certain conditions and provide a basis for self-perpetuated, protein-based infectious heritable agents (prions). Heat shock proteins acting as molecular chaperones counteract protein aggregation and influence amyloid propagation. The yeast Hsp104/Hsp70/Hsp40 chaperone complex plays a crucial role in interactions with both ordered and unordered aggregates. The main focus of this review will be on the Hsp104 chaperone, a molecular "disaggregase".

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Structure and function of Hsp78, the mitochondrial ClpB homolog

Cited by 25 publications

References 45 publications

InvestigatinghspGene Expression in Liver ofChanna striatusunder Heat Stress for Understanding the Upper Thermal Acclimation

InvestigatinghspGene Expression in Liver ofChanna striatusunder Heat Stress for Understanding the Upper Thermal Acclimation

The elusive middle domain of Hsp104 and ClpB: Location and function

Hsp104 and Prion Propagation

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