Genomic sequence encoding a heat shock-induced, RNA polymerase Ill-transcribed RNA fromTetrahymena thermophila

We determined the DNA sequence and mapped the corresponding transcripts of a genomic clone containing the Gmhsp26-A gene of soybean. This gene is homologous to the previously characterized cDNA clone pCE54 (E. Czarnecka, L. Edelman, F. Schöffl, and J. L. Key, Plant Mol. Biol. 3:45-58, 1984) and is expressed in response to a wide variety of physiological stresses including heat shock (HS). S1 nuclease mapping of transcripts and a comparison of the cDNA sequence with the genomic sequence indicated the presence of a soybean seedlings with either CdCl2 or CuSO4. Analysis of the 5' termini of transcripts indicated the presence of one major and at least two minor start sites. In each case, initiation occurred 27 to 30 base pairs downstream from a TATA-like motif, and thus each initiation site appears to be promoted by the activity of a separate subpromoter. The three subpromoters are all associated with sequences showing low homology to the HS consensus element of Drosophila melanogaster HS genes and are differentially induced in response to various stresses. Within the carboxyl-terminal half of the protein, hydropathy analysis of the deduced amino acid sequence indicated a high degree of relatedness to the small HS proteins. A comparison of the primary amino acid sequence of hsp26-A with sequences of the small HS proteins suggested that this stress protein is highly diverged and may therefore be specialized for stress adaptation in soybean.

Download Full-text

Heat-shock-induced variations in phosphorylation levels of the RNA polymerase II largest subunit may regulate its interaction with the peptidyl-prolyl-isomerase Pin1

Biochemistry and Cell Biology ◽

10.1139/o99-903v ◽

1999 ◽

Vol 77 (4) ◽

pp. 401

Author(s):

S Lavoie ◽

A Albert ◽

M Vincent

Keyword(s):

Heat Shock ◽

Rna Polymerase ◽

Rna Polymerase Ii ◽

Prolyl Isomerase ◽

Peptidyl Prolyl Isomerase

Download Full-text

Heat shock-induced alterations in phosphorylation of the largest subunit of RNA polymerase II as revealed by monoclonal antibodies CC-3 and MPM-2

Biochemistry and Cell Biology ◽

10.1139/o99-037 ◽

1999 ◽

Vol 77 (4) ◽

pp. 367-374 ◽

Cited By ~ 3

Author(s):

Sébastien B Lavoie ◽

Alexandra L Albert ◽

Alain Thibodeau ◽

Michel Vincent

Keyword(s):

Heat Shock ◽

Rna Polymerase ◽

Rna Polymerase Ii ◽

Transcriptional Activity ◽

Phosphorylation Sites ◽

Stress Genes ◽

Terminal Domain ◽

Carboxy Terminal Domain ◽

Heat Shocks ◽

Carboxy Terminal

The phosphorylation of the carboxy-terminal domain of the largest subunit of RNA polymerase II plays an important role in the regulation of transcriptional activity and is also implicated in pre-mRNA processing. Different stresses, such as a heat shock, induce a marked alteration in the phosphorylation of this domain. The expression of stress genes by RNA polymerase II, to the detriment of other genes, could be attributable to such modifications of the phosphorylation sites. Using two phosphodependent antibodies recognizing distinct hyperphosphorylated forms of RNA polymerase II largest subunit, we studied the phosphorylation state of the subunit in different species after heat shocks of varying intensities. One of these antibodies, CC-3, preferentially recognizes the carboxy-terminal domain of the largest subunit under normal conditions, but its reactivity is diminished during stress. In contrast, the other antibody used, MPM-2, demonstrated a strong reactivity after a heat shock in most species studied. Therefore, CC-3 and MPM-2 antibodies discriminate between phosphoisomers that may be functionally different. Our results further indicate that the pattern of phosphorylation of RNA polymerase II in most species varies in response to environmental stress.Key words: RNA polymerase II, heat shock, phosphorylation, CC-3, MPM-2.

Download Full-text

RNA polymerase II transcribes all of the heat shock induced genes of Drosophila melanogaster

Chromosoma ◽

10.1007/bf00344596 ◽

1982 ◽

Vol 85 (1) ◽

pp. 93-108 ◽

Cited By ~ 32

Author(s):

J. Jose Bonner ◽

Robert L. Kerby

Keyword(s):

Drosophila Melanogaster ◽

Heat Shock ◽

Rna Polymerase ◽

Rna Polymerase Ii ◽

Induced Genes

Download Full-text

Characterization of Gmhsp26-A, a stress gene encoding a divergent heat shock protein of soybean: heavy-metal-induced inhibition of intron processing

Molecular and Cellular Biology ◽

10.1128/mcb.8.3.1113-1122.1988 ◽

1988 ◽

Vol 8 (3) ◽

pp. 1113-1122

Author(s):

E Czarnecka ◽

R T Nagao ◽

J L Key ◽

W B Gurley

Keyword(s):

Amino Acid ◽

Heat Shock ◽

Amino Acid Sequence ◽

Genomic Sequence ◽

Stress Protein ◽

Initiation Site ◽

Gene Encoding ◽

S1 Nuclease ◽

Soybean Seedlings ◽

Nuclease Mapping

We determined the DNA sequence and mapped the corresponding transcripts of a genomic clone containing the Gmhsp26-A gene of soybean. This gene is homologous to the previously characterized cDNA clone pCE54 (E. Czarnecka, L. Edelman, F. Schöffl, and J. L. Key, Plant Mol. Biol. 3:45-58, 1984) and is expressed in response to a wide variety of physiological stresses including heat shock (HS). S1 nuclease mapping of transcripts and a comparison of the cDNA sequence with the genomic sequence indicated the presence of a soybean seedlings with either CdCl2 or CuSO4. Analysis of the 5' termini of transcripts indicated the presence of one major and at least two minor start sites. In each case, initiation occurred 27 to 30 base pairs downstream from a TATA-like motif, and thus each initiation site appears to be promoted by the activity of a separate subpromoter. The three subpromoters are all associated with sequences showing low homology to the HS consensus element of Drosophila melanogaster HS genes and are differentially induced in response to various stresses. Within the carboxyl-terminal half of the protein, hydropathy analysis of the deduced amino acid sequence indicated a high degree of relatedness to the small HS proteins. A comparison of the primary amino acid sequence of hsp26-A with sequences of the small HS proteins suggested that this stress protein is highly diverged and may therefore be specialized for stress adaptation in soybean.

Download Full-text

Substitution of a Highly Conserved Histidine in the Escherichia coli Heat Shock Transcription Factor, σ32, Affects Promoter Utilization In Vitro and Leads to Overexpression of the Biofilm-Associated Flu Protein In Vivo

Journal of Bacteriology ◽

10.1128/jb.01197-07 ◽

2007 ◽

Vol 189 (23) ◽

pp. 8430-8436 ◽

Cited By ~ 2

Author(s):

Olga V. Kourennaia ◽

Pieter L. deHaseth

Keyword(s):

Escherichia Coli ◽

Heat Shock ◽

Rna Polymerase ◽

Sigma Factor ◽

Stable Complex ◽

Tryptophan Residue ◽

Specific Sequence ◽

Bacterial Rna

ABSTRACT The heat shock sigma factor (σ32 in Escherichia coli) directs the bacterial RNA polymerase to promoters of a specific sequence to form a stable complex, competent to initiate transcription of genes whose products mitigate the effects of exposure of the cell to high temperatures. The histidine at position 107 of σ32 is at the homologous position of a tryptophan residue at position 433 of the main sigma factor of E. coli, σ70. This tryptophan is essential for the strand separation step leading to the formation of the initiation-competent RNA polymerase-promoter complex. The heat shock sigma factors of all gammaproteobacteria sequenced have a histidine at this position, while in the alpha- and deltaproteobacteria, it is a tryptophan. In vitro the alanine-for-histidine substitution at position 107 (H107A) destabilizes complexes between the GroE promoter and RNA polymerase containing σ32, implying that H107 plays a role in formation or maintenance of the strand-separated complex. In vivo, the H107A substitution in σ32 impedes recovery from heat shock (exposure to 42°C), and it also leads to overexpression at lower temperatures (30°C) of the Flu protein, which is associated with biofilm formation.

Download Full-text