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

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

A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1

1999 ◽  
Vol 112 (15) ◽  
pp. 2493-2500 ◽  
Author(s):  
A. Albert ◽  
S. Lavoie ◽  
M. Vincent
Keyword(s):  
Monoclonal Antibody ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Matrix Protein ◽  
Large Subunit ◽  
Dependent Manner ◽  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase ◽  
M Phase ◽  
Hyperphosphorylated Form

The monoclonal antibody MPM-2 recognizes a subset of M phase phosphoproteins in a phosphorylation-dependent manner. It is believed that phosphorylation at MPM-2 antigenic sites could regulate mitotic events since most of the MPM-2 antigens identified to date have M phase functions. In addition, many of these proteins are substrates of the mitotic regulator Pin1, a peptidyl-prolyl isomerase which is present throughout the cell cycle and which is thought to alter its mitotic targets by changing their conformation. In interphase cells, most MPM-2 reactivity is confined to nuclear speckles. We report here that a hyperphosphorylated form of the RNA polymerase II largest subunit is the major MPM-2 interphase antigen. These findings were made possible by the availability of another monoclonal antibody, CC-3, that was previously used to identify a 255 kDa nuclear matrix protein associated with spliceosomal components as a hyperphosphorylated form of the RNA polymerase II largest subunit. MPM-2 recognizes a phosphoepitope of the large subunit that becomes hyperphosphorylated upon heat shock in contrast to the phosphoepitope defined by CC-3, whose reactivity is diminished by the heat treatment. Therefore, these two antibodies may discriminate between distinct functional forms of RNA polymerase II. We also show that RNA polymerase II large subunit interacts with Pin1 in HeLa cells. Pin1 may thus regulate transcriptional and post-transcriptional events by catalyzing phosphorylation-dependent conformational changes of the large RNA polymerase II subunit.

scholarly journals The Peptidyl Prolyl Isomerase Rrd1 Regulates the Elongation of RNA Polymerase II during Transcriptional Stresses

PLoS ONE ◽  
2011 ◽  
Vol 6 (8) ◽  
pp. e23159 ◽  
Author(s):  
Jeremie Poschmann ◽  
Simon Drouin ◽  
Pierre-Etienne Jacques ◽  
Karima El Fadili ◽  
Michael Newmarch ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase

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

1999 ◽  
Vol 77 (4) ◽  
pp. 367-374 ◽  
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.

scholarly journals Heat-shock inactivation of the TFIIH-associated kinase and change in the phosphorylation sites on the C-terminal domain of RNA polymerase II

1997 ◽  
Vol 25 (4) ◽  
pp. 694-700 ◽  
Author(s):  
M.-F. Dubois ◽  
M. Vincent ◽  
M. Vigneron ◽  
J. Adamczewski ◽  
J.-M. Egly ◽  
...  
Keyword(s):  
Heat Shock ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Phosphorylation Sites ◽  
Terminal Domain

scholarly journals Fcp1 Dephosphorylation of the RNA Polymerase II C-Terminal Domain Is Required for Efficient Transcription of Heat Shock Genes

2012 ◽  
Vol 32 (17) ◽  
pp. 3428-3437 ◽  
Author(s):  
N. J. Fuda ◽  
M. S. Buckley ◽  
W. Wei ◽  
L. J. Core ◽  
C. T. Waters ◽  
...  
Keyword(s):  
Heat Shock ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Heat Shock Genes ◽  
Terminal Domain

scholarly journals Rapid changes in Drosophila transcription after an instantaneous heat shock.

1993 ◽  
Vol 13 (6) ◽  
pp. 3456-3463 ◽  
Author(s):  
T O'Brien ◽  
J T Lis
Keyword(s):  
Heat Shock ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Uv Light ◽  
Hsp70 Gene ◽  
Rapid Induction ◽  
Rapid Changes ◽  
Rapid Activation ◽  
Kinetics Of

Heat shock rapidly activates expression of some genes and represses others. The kinetics of changes in RNA polymerase distribution on heat shock-modulated genes provides a framework for evaluating the mechanisms of activation and repression of transcription. Here, using two methods, we examined the changes in RNA polymerase II association on a set of Drosophila genes at 30-s intervals following an instantaneous heat shock. In the first method, Drosophila Schneider line 2 cells were quickly frozen to halt transcription, and polymerase distribution was analyzed by a nuclear run-on assay. RNA polymerase transcription at the 5' end of the hsp70 gene could be detected within 30 to 60 s of induction, and by 120 s the first wave of polymerase could already be detected near the 3' end of the gene. A similar rapid induction was found for the small heat shock genes (hsp22, hsp23, hsp26, and hsp27). In contrast to this rapid activation, transcription of the histone H1 gene was found to be rapidly repressed, with transcription reduced by approximately 90% within 300 s of heat shock. Similar results were obtained by an in vivo UV cross-linking assay. In this second method, cell samples removed at 30-s intervals were irradiated with 40-microseconds bursts of UV light from a Xenon flash lamp, and the distribution of polymerase was examined by precipitating UV cross-linked protein-DNA complexes with an antibody to RNA polymerase II. Both approaches also showed the in vivo rate of movement of the first wave of RNA polymerase through the hsp70 gene to be approximately 1.2 kb/min.

Correlation between the activity of a 5,6-dichloro-1-β-D-ribofuranosylbenzimidazole-insensitive puff and the synthesis of major heat-shock polypeptide, hsp70, in Chironomus thummi

1988 ◽  
Vol 66 (11) ◽  
pp. 1177-1185 ◽  
Author(s):  
D. Barettino ◽  
G. Morcillo ◽  
J. L. Díez ◽  
M. T. Carretero ◽  
M. J. Carmona
Keyword(s):  
Heat Shock ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Specific Inhibitor ◽  
In Vitro Transcription ◽  
The Other ◽  
Low Salt ◽  
Transcription Inhibitor ◽  
Chironomus Thummi

The induction of puff III-A3b, a major heat-shock puff in Chironomus thummi salivary cells, was insensitive to the transcription inhibitor 5,6-dichloro-1-β-D-ribofuranosylbenzimidazole (DRB), whereas no transcriptional activity could be detected at the other heat-shock puffs in the presence of this drug. In these conditions, a polypeptide with the same Mr and isoform pattern as those of the major heat-shock polypeptide, hsp70, was synthesized. These results suggest that hsp70 is encoded by locus III-A3b. In addition to DRB insensitivity, incorporation of [3H]UTP on puff III-A3b took place in an in vitro transcription assay under low-salt conditions (100 mM NaCl); no labelling could be detected at the other heat-shock puffs under these conditions. Although DRB has been reported as a specific inhibitor of RNA polymerase II-directed transcription, and although the low-salt conditions were not propitious for the activity of this enzyme, RNA polymerase II was detected on puff III-A3b and on the other heat-shock puffs by immunofluorescence with anti-RNA polymerase II antibodies.

scholarly journals Multiple Roles for the Ess1 Prolyl Isomerase in the RNA Polymerase II Transcription Cycle

2012 ◽  
Vol 32 (17) ◽  
pp. 3594-3607 ◽  
Author(s):  
Z. Ma ◽  
D. Atencio ◽  
C. Barnes ◽  
H. DeFiglio ◽  
S. D. Hanes
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Multiple Roles ◽  
Prolyl Isomerase ◽  
Rna Polymerase Ii Transcription ◽  
Transcription Cycle
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