Multiple functions of<i>Drosophila</i>heat shock transcription factor<i>in vivo</i>

Jedlicka, Paul; Mortin, Mark A.; Wu, Carl

doi:10.1093/emboj/16.9.2452

Cited by 274 publications

(261 citation statements)

References 89 publications

Supporting

Mentioning

245

Contrasting

Unclassified

Order By: Relevance

“…Analyses of genetic variation that are expressed only under specific environmental conditions permit a detailed functional analysis of major genetic defects that are otherwise difficult to study (Jedlicka et al, 1997;Willis et al, 2006). Environmentally conditioned mutations covering the whole genome can easily be obtained; in particular, the fruitfly (Drosophila melanogaster) has been used extensively as a model organism in this context (Suzuki, 1970;Tasaka and Suzuki, 1973;Arking, 1975;Mitchell and Petersen, 1982;Homyk et al, 1986).…”

Section: Introductionmentioning

confidence: 99%

Proteomic characterization of a temperature-sensitive conditional lethal in Drosophila melanogaster

et al. 2009

View full text Add to dashboard Cite

Genetic variation that is expressed only under specific environmental conditions can contribute to additional adverse effects of inbreeding if environmental conditions change. We present a proteomic characterization of a conditional lethal found in an inbred line of Drosophila melanogaster. The lethal effect is apparent as a large increase in early mortality at the restrictive temperature (29 1C) as opposed to normal survival at the permissive temperature (20 1C). The increased mortality in response to the restrictive temperature is probably caused by a single recessive major locus. A quantitative trait locus (QTL) region segregating variation affecting the lethal effect has been identified, allowing for a separation of primary/causal effects and secondary consequences in the proteome expression patterns observed. In this study, the proteomic response to the restrictive temperature in the lethal-line (L-line) was compared with the response in an inbred-control-line (IC-line) and an outbred-control-line (OC-line). Quantitative protein changes were detected using isobaric tags for relative and absolute quantitation (iTRAQ) two-dimensional liquid chromatography-tandem mass spectrometry. In all, 45 proteins were found to be significantly differently regulated in response to the restrictive temperature in the L-line as compared with the IC-line. No proteins were significantly differently regulated between the IC-line and the OC-line, verifying that differential protein regulation was specific to a genetic defect in the L-line. Proteins associated with oxidative phosphorylation and mitochondria were significantly overrepresented within the list of differentially expressed proteins. Proteins related to muscle contraction were also found to be differentially expressed in the L-line in response to the restrictive temperature, supporting phenotypic observations of moribund muscle hypercontraction.

show abstract

Section: Introductionmentioning

confidence: 99%

Proteomic characterization of a temperature-sensitive conditional lethal in Drosophila melanogaster

et al. 2009

View full text Add to dashboard Cite

show abstract

“…1 Although in some systems, as in Drosophila melanogaster, this regulation involves a single HSF (1), multigenic families of HSFs participate in vertebrate and in plant systems. These families have different sizes, which, together with particular gene expression and activation patterns for the HSFs, might have consequences in the degree of overlapping of regulatory functions mediated by these factors.…”

mentioning

confidence: 99%

A Seed-specific Heat-shock Transcription Factor Involved in Developmental Regulation during Embryogenesis in Sunflower

Almoguera

Rojas²,

Díaz‐Martín³

et al. 2002

Journal of Biological Chemistry

115

View full text Add to dashboard Cite

We report the cloning and functional characterization of the first heat-shock transcription factor that is specifically expressed during embryogenesis in the absence of environmental stress. In sunflower embryos this factor, HaHSFA9, trans-activated promoters with poor consensus heat-shock cis-elements, including that of the seed-specific Hahsp17.6G1 gene. Mutations that improved the heat-shock cis-element consensus at the Hahsp17.7G4 promoter impaired transient activation by HaHSFA9 in sunflower embryos. The same mutations did not affect heat-shock-induced gene expression of this promoter in transgenic tobacco plants but reduced the developmental activation by endogenous heat-shock transcription factors (HSFs) in seeds. Sunflower, and perhaps other plants such as tobacco, differs from the vertebrate animal systems in having at least one specialized HSF with expression and (or) activation patterns strictly restricted to embryos. Our results strongly indicate that HaHSFA9 is a transcription factor critically involved in the developmental activation of Hahsp17.6G1 and in that of similar target genes as Hahsp17.7G4.In eukaryotes, the heat-shock response and some developmental processes are under the control of a family of conserved DNA-binding proteins known as the heat-shock transcription factors (HSFs). 1 Although in some systems, as in Drosophila melanogaster, this regulation involves a single HSF (1), multigenic families of HSFs participate in vertebrate and in plant systems. These families have different sizes, which, together with particular gene expression and activation patterns for the HSFs, might have consequences in the degree of overlapping of regulatory functions mediated by these factors. The specific role of the different HSFs is mostly unknown, particularly for the plant HSFs, and for involvement in developmental processes, as the regulation of gene expression during embryogenesis (See for example, Ref. 2 and the reviews in Refs. 3 and 4).In vertebrate systems, three different HSFs (HSF1, HSF2, and HSF3) have ubiquitous expression patterns (for example, Refs. 5 and 6 and the review in Ref.3). A fourth HSF found in humans displays tissue-specific expression patterns, which suggested specialized functions but not related to embryogenesis (HSF4, Ref. 7). Plants contain the highest number of HSF genes in eukaryotes. This is inferred from in silico analyses from the fully sequenced Arabidopsis thaliana model and from functional analyses of different cloned HSFs in tomato, Arabidopsis, and other plants (reviewed in Refs. 4 and 8 and references therein). Plant HSFs share unique structural and phylogenetic relationships compared with the vertebrate HSFs (9). Fifteen of the 21 putative HSFs from A. thaliana thus contain an insertion of 21 amino acid residues in the oligomerization domain (characteristic of the plant class A HSFs), whereas class B HSFs have no such insertion. Gene expression studies for plant HSFs are very scarce, with only fragmentary data at the mRNA level and even scarcer reports for prote...

show abstract

“…The HSF1 gene is essential: it is required for cell viability in yeast and is also strongly conserved throughout the eukaryotic kingdom (Wiederrecht et al, 1988;Jedlicka et al, 1997). Temperature-sensitive alleles of HSF1 are available, allowing easy phenotypic comparison against our mislocalized Hsf1p mutants.…”

Section: Drug-induced Mislocalization Of An Essential Gene Mimics a Lmentioning

confidence: 99%

A small molecule‐directed approach to control protein localization and function

Geda

Patury

et al. 2008

Yeast

View full text Add to dashboard Cite

Protein localization is tightly linked with function, such that the subcellular distribution of a protein serves as an important control point regulating activity. Exploiting this regulatory mechanism, we present here a general approach by which protein location, and hence function, may be controlled on demand in the budding yeast. In this system a small molecule, rapamycin, is used to temporarily recruit a strong cellular address signal to the target protein, placing subcellular localization under control of the selective chemical stimulus. The kinetics of this system are rapid: rapamycin-directed nucleo-cytoplasmic transport is evident 10-12 min posttreatment and the process is reversible upon removal of rapamycin. Accordingly, we envision this platform as a promising approach for the systematic construction of conditional loss-of-function mutants. As proof of principle, we used this system to direct nuclear export of the essential heat shock transcription factor Hsf1p, thereby mimicking the cell-cycle arrest phenotype of an hsf1 temperature-sensitive mutant. Our drug-induced localization platform also provides a method by which protein localization can be uncoupled from endogenous cell signalling events, addressing the necessity or sufficiency of a given localization shift for a particular cell process. To illustrate, we directed the nuclear import of the calcineurin-dependent transcription factor Crz1p in the absence of native stimuli; this analysis directly substantiates that nuclear translocation of this protein is insufficient for its transcriptional activity. In total, this technology represents a powerful method for the generation of conditional alleles and directed mislocalization studies in yeast, with potential applicability on a genome-wide scale.

show abstract

Multiple functions ofDrosophilaheat shock transcription factorin vivo

Cited by 274 publications

References 89 publications

Proteomic characterization of a temperature-sensitive conditional lethal in Drosophila melanogaster

Proteomic characterization of a temperature-sensitive conditional lethal in Drosophila melanogaster

A Seed-specific Heat-shock Transcription Factor Involved in Developmental Regulation during Embryogenesis in Sunflower

A small molecule‐directed approach to control protein localization and function

Contact Info

Product

Resources

About