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Grandemange, Sylvie; Schaller, Sophie; Yamano, Shigeru; Manoir, Stanislas du; Shpakovski, George V.; Matteï, Marie‐Geneviève; Kédinger, Claude; Vigneron, Marc

doi:10.1186/1471-2199-2-14

Cited by 15 publications

(14 citation statements)

References 38 publications

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“…Here, we provide the first evidence about in vivo functional distinction between the previously discovered [20][21][22][23][24][25][26] distinct human isoforms of the hRPB11 (POLR2J) subunit of RNA polymerase II of Homo sapiens: The strength of the hRPB11-ATF4 interaction in corresponding transcription complexes appeared to be isoform-specific.…”

Section: Introductionmentioning

confidence: 74%

“…Previously, we have shown that, in drastic difference with all other species, small indispensable subunit Rpb11 of RNA polymerase II is encoded in Homo sapiens by four different genes located on chromosome 7 [20,21]. One gene, POLR2J1 (~5.5 kb long), is orthologous to the corresponding rpb11 genes in other species and encodes the usual (trivial), main isoform of hRPB11 (POLR2J) subunit called hRPB11a (117 aa long) which, as judged by its evolutionary history, is the subject of strong purifying selection because is strictly conserved in all warm-blooded animals.…”

Section: Resultsmentioning

confidence: 99%

“…In humans, a gene family has been identified that potentially encodes several hRPB11 (POLR2J) proteins differing mainly in their C-terminal regions [20][21][22][23]. The POLR2J1 (RPB11a) gene encodes hRPB11a subunit representing the major component of mammalian RNAPII complex.…”

Section: Introductionmentioning

confidence: 99%

“…The POLR2J1 (RPB11a) gene encodes hRPB11a subunit representing the major component of mammalian RNAPII complex. Other members of the family, the POLR2J2 (RPB11b) and POLR2J3 (RPB11c) genes, yield several minor mRNAs resulting from alternative splicing [20,21]. Whether the transcripts of the POLR2J2 (RPB11b) gene are translated remain to be established.…”

Section: Introductionmentioning

confidence: 99%

“…Whether the transcripts of the POLR2J2 (RPB11b) gene are translated remain to be established. Remarkably, using complementation assay, it was demonstrated that only minor isoform hRPB11bα (the product of expression of the POLR2J2 gene) is functional in yeast whereas the major (the true orthologue of Rpb11 from all other species) hRPB11a is not [20]. Obviously, the existence of a variety of human-specific subunit isoforms indicates the fact that the more intricate mechanisms for regulation of transcription in human cells have evolved [24][25][26].…”

Section: Introductionmentioning

confidence: 99%

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The Human Isoform of RNA Polymerase II Subunit hRPB11bα Specifically Interacts with Transcription Factor ATF4

Proshkin

Shematorova

Shpakovski

2019

IJMS

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Rpb11 subunit of RNA polymerase II of Eukaryotes is related to N-terminal domain of eubacterial α subunit and forms a complex with Rpb3 subunit analogous to prokaryotic α2 homodimer, which is involved in RNA polymerase assembly and promoter recognition. In humans, a POLR2J gene family has been identified that potentially encodes several hRPB11 proteins differing mainly in their short C-terminal regions. The functions of the different human specific isoforms are still mainly unknown. To further characterize the minor human specific isoform of RNA polymerase II subunit hRPB11bα, the only one from hRPB11 (POLR2J) homologues that can replace its yeast counterpart in vivo, we used it as bait in a yeast two-hybrid screening of a human fetal brain cDNA library. By this analysis and subsequent co-purification assay in vitro, we identified transcription factor ATF4 as a prominent partner of the minor RNA polymerase II (RNAP II) subunit hRPB11bα. We demonstrated that the hRPB11bα interacts with leucine b-Zip domain located on the C-terminal part of ATF4. Overexpression of ATF4 activated the reporter more than 10-fold whereas co-transfection of hRPB11bα resulted in a 2.5-fold enhancement of ATF4 activation. Our data indicate that the mode of interaction of human RNAP II main (containing major for of hRPB11 subunit) and minor (containing hRPB11bα isoform of POLR2J subunit) transcription enzymes with ATF4 is certainly different in the two complexes involving hRPB3–ATF4 (not hRPB11a–ATF4) and hRpb11bα–ATF4 platforms in the first and the second case, respectively. The interaction of hRPB11bα and ATF4 appears to be necessary for the activation of RNA polymerase II containing the minor isoform of the hRPB11 subunit (POLR2J) on gene promoters regulated by this transcription factor. ATF4 activates transcription by directly contacting RNA polymerase II in the region of the heterodimer of α-like subunits (Rpb3–Rpb11) without involving a Mediator, which provides fast and highly effective activation of transcription of the desired genes. In RNA polymerase II of Homo sapiens that contains plural isoforms of the subunit hRPB11 (POLR2J), the strength of the hRPB11–ATF4 interaction appeared to be isoform-specific, providing the first functional distinction between the previously discovered human forms of the Rpb11 subunit.

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Section: Introductionmentioning

confidence: 74%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The Human Isoform of RNA Polymerase II Subunit hRPB11bα Specifically Interacts with Transcription Factor ATF4

Proshkin

Shematorova

Shpakovski

2019

IJMS

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Emerging roles of AATF: Checkpoint signaling and beyond

Srinivas

Suresh

Mirshahi

et al. 2020

Journal Cellular Physiology

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Apoptosis antagonizing transcription factor (AATF), an interacting partner of RNA polymerase II is a multifunctional protein that is highly conserved in eukaryotes. In addition to the regulation of gene expression as a transcriptional coactivator, AATF is shown to play a dual role in regulating the cell cycle by displacing histone deacetylases 1 (HDAC1) from the retinoblastoma‐E2F transcription factor (Rb‐E2F) complex and also from the specificity protein 1 (Sp1) transcription factor responsible for p21 expression, thereby ensuring cell proliferation and growth arrest, respectively, at different checkpoints of the cell cycle. Notably, AATF has emerged as one of the most important modulators of various cellular responses such as proliferation, apoptosis, and survival. Studies have demonstrated that AATF protects cells from multiple stress stimuli such as DNA damage, ER stress, hypoxia, or glucose deprivation by inducing cell cycle arrest, autophagy, or apoptosis inhibition. Furthermore, AATF serves as a critical regulator in various cancers and promotes tumorigenesis by protecting cancer cells from apoptosis induction, favoring cell proliferation, or promoting cell survival by autophagy. Recent studies have demonstrated the key role of AATF in ribosome biosynthesis and have also provided insights into the mechanistic role of AATF, offering impressive cytoprotection in myocardial infarction, neurologic diseases, and nephronophthisis. In this review, we will provide a comprehensive overview of the role of AATF and shed light on its emerging roles underlining the potential use of AATF as a novel biomarker and as an effective therapeutic target.

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The Thymocyte-Specific MAR Binding Protein, SATB1, Interacts in Vitro with a Novel Variant of DNA-Directed RNA Polymerase II, Subunit 11

Durrin

Krontiris

2002

Genomics

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Abstract: Background: The sequences encoding the yeast RNA polymerase II (RPB) subunits are single copy genes.

Cited by 15 publications

References 38 publications

The Human Isoform of RNA Polymerase II Subunit hRPB11bα Specifically Interacts with Transcription Factor ATF4

The Human Isoform of RNA Polymerase II Subunit hRPB11bα Specifically Interacts with Transcription Factor ATF4

Emerging roles of AATF: Checkpoint signaling and beyond

The Thymocyte-Specific MAR Binding Protein, SATB1, Interacts in Vitro with a Novel Variant of DNA-Directed RNA Polymerase II, Subunit 11

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