scholarly journals Displacement of Histones at Promoters of Saccharomyces cerevisiae Heat Shock Genes Is Differentially Associated with Histone H3 Acetylation

2006 ◽  
Vol 26 (20) ◽  
pp. 7587-7600 ◽  
Author(s):  
T. Y. Erkina ◽  
A. M. Erkine
Keyword(s):  
Heat Shock ◽  
Chromatin Remodeling ◽  
Histone H3 ◽  
Heat Shock Gene ◽  
Gene Promoters ◽  
Heat Shock Genes ◽  
Factors Affecting ◽  
Histone H3 Acetylation ◽  
Shock Gene ◽  
H3 Acetylation

ABSTRACT Chromatin remodeling at promoters of activated genes spans from mild histone modifications to outright displacement of nucleosomes in trans. Factors affecting these events are not always clear. Our results indicate that histone H3 acetylation associated with histone displacement differs drastically even between promoters of such closely related heat shock genes as HSP12, SSA4, and HSP82. The HSP12 promoter, with the highest level of histone displacement, showed the highest level of H3 acetylation, while the SSA4 promoter, with a lower histone displacement, showed only modest H3 acetylation. Moreover, for the HSP12 promoter, the level of acetylated H3 is temporarily increased prior to nucleosome departure. Individual promoters in strains expressing truncated versions of heat shock factor (HSF) showed that deletion of either one of two activating regions in HSF led to the diminished histone displacement and correspondingly lower H3 acetylation. The deletion of both regions simultaneously severely decreased histone displacement for all promoters tested, showing the dependence of these processes on HSF. The level of histone H3 acetylation at individual promoters in strains expressing truncated HSF also correlated with the extent of histone displacement. The beginning of chromatin remodeling coincides with the polymerase II loading on heat shock gene promoters and is regulated either by HSF binding or activation of preloaded HSF.

scholarly journals Three light-inducible heat shock genes of Chlamydomonas reinhardtii.

1989 ◽  
Vol 9 (9) ◽  
pp. 3911-3918 ◽  
Author(s):  
E D von Gromoff ◽  
U Treier ◽  
C F Beck
Keyword(s):  
Thermal Stress ◽  
Elevated Temperature ◽  
Heat Shock ◽  
Chlamydomonas Reinhardtii ◽  
Heat Shock Gene ◽  
Mrna Levels ◽  
Heat Shock Genes ◽  
Drastic Increase ◽  
Shock Gene

Genomic clones representing three Chlamydomonas reinhardtii genes homologous to the Drosophila hsp70 heat shock gene were isolated. The mRNAs of genes hsp68, hsp70, and hsp80 could be translated in vitro into proteins of Mr 68,000, 70,000, and 80,000, respectively. Transcription of these genes increased dramatically upon heat shock, and the corresponding mRNAs rapidly accumulated, reaching a peak at around 30 min after a shift to the elevated temperature. Light also induced the accumulation of the mRNAs encoded by these heat shock genes. A shift of dark-grown cells to light resulted in a drastic increase in mRNA levels, which reached a maximum at around 1 h after the shift. Thus, in Chlamydomonas, expression of hsp70-homologous heat shock genes appears to be regulated by thermal stress and light.

Three light-inducible heat shock genes of Chlamydomonas reinhardtii

1989 ◽  
Vol 9 (9) ◽  
pp. 3911-3918
Author(s):  
E D von Gromoff ◽  
U Treier ◽  
C F Beck
Keyword(s):  
Thermal Stress ◽  
Elevated Temperature ◽  
Heat Shock ◽  
Chlamydomonas Reinhardtii ◽  
Heat Shock Gene ◽  
Mrna Levels ◽  
Heat Shock Genes ◽  
Drastic Increase ◽  
Shock Gene

Genomic clones representing three Chlamydomonas reinhardtii genes homologous to the Drosophila hsp70 heat shock gene were isolated. The mRNAs of genes hsp68, hsp70, and hsp80 could be translated in vitro into proteins of Mr 68,000, 70,000, and 80,000, respectively. Transcription of these genes increased dramatically upon heat shock, and the corresponding mRNAs rapidly accumulated, reaching a peak at around 30 min after a shift to the elevated temperature. Light also induced the accumulation of the mRNAs encoded by these heat shock genes. A shift of dark-grown cells to light resulted in a drastic increase in mRNA levels, which reached a maximum at around 1 h after the shift. Thus, in Chlamydomonas, expression of hsp70-homologous heat shock genes appears to be regulated by thermal stress and light.

scholarly journals Acetylation of Rsc4p by Gcn5p Is Essential in the Absence of Histone H3 Acetylation

2008 ◽  
Vol 28 (23) ◽  
pp. 6967-6972 ◽  
Author(s):  
Jennifer K. Choi ◽  
Daniel E. Grimes ◽  
Keegan M. Rowe ◽  
LeAnn J. Howe
Keyword(s):  
Chromatin Remodeling ◽  
Histone H3 ◽  
Growth Defect ◽  
Chromatin Remodeling Complex ◽  
Histone H3 Acetylation ◽  
Phenotype Comparison ◽  
A Subunit ◽  
Redundant Functions ◽  
H3 Acetylation ◽  
First Time

ABSTRACT Rsc4p, a subunit of the RSC chromatin-remodeling complex, is acetylated at lysine 25 by Gcn5p, a well-characterized histone acetyltransferase (HAT). Mutation of lysine 25 does not result in a significant growth defect, and therefore whether this modification is important for the function of the essential RSC complex was unknown. In a search to uncover the molecular basis for the lethality resulting from loss of multiple histone H3-specific HATs, we determined that loss of Rsc4p acetylation is lethal in strains lacking histone H3 acetylation. Phenotype comparison of mutants with arginine and glutamine substitutions of acetylatable lysines within the histone H3 tail suggests that it is a failure to neutralize the charge of the H3 tail that is lethal in strains lacking Rsc4p acetylation. We also demonstrate that Rsc4p acetylation does not require any of the known Gcn5p-dependent HAT complexes and thus represents a truly novel function for Gcn5p. These results demonstrate for the first time the vital and yet redundant functions of histone H3 and Rsc4p acetylation in maintaining cell viability.

Reduction in Histone H3 Acetylation and Chromatin Remodeling in Corneas of Alloxan-Induced Diabetic Rats

Cornea ◽  
2018 ◽  
Vol 37 (5) ◽  
pp. 624-632 ◽  
Author(s):  
Karina E. Herencia-Bueno ◽  
Marcela Aldrovani ◽  
Roberta M. Crivelaro ◽  
Roberto Thiesen ◽  
Alexandre A. F. Barros-Sobrinho ◽  
...  
Keyword(s):  
Chromatin Remodeling ◽  
Histone H3 ◽  
Diabetic Rats ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

scholarly journals α-Synuclein A53T Binds to Transcriptional Adapter 2-Alpha and Blocks Histone H3 Acetylation

2021 ◽  
Vol 22 (10) ◽  
pp. 5392
Author(s):  
Ji-Yeong Lee ◽  
Hanna Kim ◽  
Areum Jo ◽  
Rin Khang ◽  
Chi-Hu Park ◽  
...  
Keyword(s):  
Gene Regulation ◽  
Chromatin Remodeling ◽  
Dopaminergic Neurons ◽  
Histone H3 ◽  
Lewy Bodies ◽  
Wild Type ◽  
Binding Partner ◽  
Amyloidogenic Protein ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

α-Synuclein (α-syn) is a hallmark amyloidogenic protein component of Lewy bodies in dopaminergic neurons affected by Parkinson’s disease (PD). Despite the multi-faceted gene regulation of α-syn in the nucleus, the mechanism underlying α-syn crosstalk in chromatin remodeling in PD pathogenesis remains elusive. Here, we identified transcriptional adapter 2-alpha (TADA2a) as a novel binding partner of α-syn using the BioID system. TADA2a is a component of the p300/CBP-associated factor and is related to histone H3/H4 acetylation. We found that α-syn A53T was more preferentially localized in the nucleus than the α-syn wild-type (WT), leading to a stronger disturbance of TADA2a. Indeed, α-syn A53T significantly reduced the level of histone H3 acetylation in SH-SY5Y cells; its reduction was also evident in the striatum (STR) and substantia nigra (SN) of mice that were stereotaxically injected with α-syn preformed fibrils (PFFs). Interestingly, α-syn PFF injection resulted in a decrease in TADA2a in the STR and SN of α-syn PFF-injected mice. Furthermore, the levels of TADA2a and acetylated histone H3 were significantly decreased in the SN of patients with PD. Therefore, histone modification through α-syn A53T-TADA2a interaction may be associated with α-syn-mediated neurotoxicity in PD pathology.

scholarly journals Consensus sequence for Escherichia coli heat shock gene promoters.

1985 ◽  
Vol 82 (9) ◽  
pp. 2679-2683 ◽  
Author(s):  
D. W. Cowing ◽  
J. C. Bardwell ◽  
E. A. Craig ◽  
C. Woolford ◽  
R. W. Hendrix ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Consensus Sequence ◽  
Heat Shock Gene ◽  
Gene Promoters ◽  
Shock Gene

scholarly journals Regulation of the Bacillus subtilis Heat Shock Gene htpG Is under Positive Control

2003 ◽  
Vol 185 (2) ◽  
pp. 466-474 ◽  
Author(s):  
Saskia Versteeg ◽  
Angelika Escher ◽  
Andy Wende ◽  
Thomas Wiegert ◽  
Wolfgang Schumann
Keyword(s):  
Bacillus Subtilis ◽  
Heat Shock ◽  
Dna Sequence ◽  
Positive Control ◽  
Absolute Temperature ◽  
Heat Shock Gene ◽  
Transcriptional Repressors ◽  
Heat Shock Genes ◽  
Regulation Mechanisms ◽  
Shock Gene

ABSTRACT The heat shock genes of Bacillus subtilis are assigned to four classes on the basis of their regulation mechanisms. While classes I and III are negatively controlled by two different transcriptional repressors, class II is regulated by the alternative sigma factor σB. All heat shock genes with unidentified regulatory mechanisms, among them htpG, constitute class IV. Here, we show that expression of htpG is under positive control. We identified a DNA sequence (GAAAAGG) located downstream of the σA-dependent promoter of htpG. The heat inducibility of the promoter could be destroyed by inversion, nucleotide replacements, or removal of this DNA sequence. Fusion of this sequence to the vegetative lepA promoter conferred heat inducibility. Furthermore, we were able to show that the heat induction factor is dependent on the absolute temperature rather than the temperature increment and that nonnative proteins within the cytoplasm fail to induce htpG.

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