TY - JOUR AU - Újfaludi, Zsuzsanna AU - Tuzesi, Agota AU - Majoros, Hajnalka AU - Rothler, Bálint AU - Pankotai, Tibor AU - Boros, Imre Miklós TI - Coordinated activation of a cluster of MMP genes in response to UVB radiation JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 8 PY - 2018 IS - 1 PG - 10 SN - 2045-2322 DO - 10.1038/s41598-018-20999-6 UR - https://m2.mtmt.hu/api/publication/3333944 ID - 3333944 AB - Ultraviolet (UV) B radiation is a dangerous environmental stressor, which can lead to photoaging, inflammation, immune suppression and tumour formation. A recent report has shown the transcriptional activation of several skin-specific genes including matrix metalloproteases (MMPs) in response to UV irradiation. Here, we use a novel human keratinocyte model, HKerE6SFM, to demonstrate that UVB activates the transcription of most members of the 11q22.3 MMP gene cluster including MMP13, MMP12, MMP3, MMP1 and MMP10. Curiously, the expression of the well-characterized UVB-inducible MMP9, which is located outside of the cluster, remains unchanged. In accordance with the increased expression of the MMP gene cluster upon UVB irradiation, RNA polymerase II showed increased occupancy at their promoters following UVB irradiation. The results also demonstrate increased acetylated histone H3K9 levels at the promoters of the MMP13, MMP12, MMP3, MMP1 and MMP10 genes. These findings suggest a coordinated transcriptional activation of genes in the MMP cluster at 11q22.3 and that acetylation of histone H3 at lysine 9 has an important role in the UVB-dependent enhancement of transcription of MMP genes in this region. LA - English DB - MTMT ER - TY - JOUR AU - Borsos, Barbara Nikolett AU - Huliák, Ildikó AU - Majoros, Hajnalka AU - Újfaludi, Zsuzsanna AU - Gyenis, A AU - Pukler, P AU - Boros, Imre Miklós AU - Pankotai, Tibor TI - Human p53 interacts with the elongating RNAPII complex and is required for the release of actinomycin D induced transcription blockage JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 7 PY - 2017 PG - 11 SN - 2045-2322 DO - 10.1038/srep40960 UR - https://m2.mtmt.hu/api/publication/3170378 ID - 3170378 N1 - Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, 6726, Hungary Department of Molecular Genetics, Erasmus University Medical Centre, Rotterdam, PO Box 2040CA 3000, Netherlands Institute of Biochemistry, Biological Research Centre, Szeged, 6726, Hungary Cited By :4 Export Date: 30 August 2019 Correspondence Address: Pankotai, T.; Department of Biochemistry and Molecular Biology, University of SzegedHungary; email: pankotai@bio.u-szeged.hu Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, 6726, Hungary Department of Molecular Genetics, Erasmus University Medical Centre, Rotterdam, PO Box 2040CA 3000, Netherlands Institute of Biochemistry, Biological Research Centre, Szeged, 6726, Hungary Cited By :4 Export Date: 31 August 2019 Correspondence Address: Pankotai, T.; Department of Biochemistry and Molecular Biology, University of SzegedHungary; email: pankotai@bio.u-szeged.hu Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, 6726, Hungary Department of Molecular Genetics, Erasmus University Medical Centre, Rotterdam, PO Box 2040CA 3000, Netherlands Institute of Biochemistry, Biological Research Centre, Szeged, 6726, Hungary Cited By :4 Export Date: 2 September 2019 Correspondence Address: Pankotai, T.; Department of Biochemistry and Molecular Biology, University of SzegedHungary; email: pankotai@bio.u-szeged.hu Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, 6726, Hungary Department of Molecular Genetics, Erasmus University Medical Centre, Rotterdam, PO Box 2040CA 3000, Netherlands Institute of Biochemistry, Biological Research Centre, Szeged, 6726, Hungary Cited By :5 Export Date: 6 November 2019 Correspondence Address: Pankotai, T.; Department of Biochemistry and Molecular Biology, University of SzegedHungary; email: pankotai@bio.u-szeged.hu Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, 6726, Hungary Department of Molecular Genetics, Erasmus University Medical Centre, Rotterdam, PO Box 2040CA 3000, Netherlands Institute of Biochemistry, Biological Research Centre, Szeged, 6726, Hungary Cited By :5 Export Date: 12 February 2020 Correspondence Address: Pankotai, T.; Department of Biochemistry and Molecular Biology, University of SzegedHungary; email: pankotai@bio.u-szeged.hu Funding Agency and Grant Number: Kutatoegyetemi es Kivalosagi EMMI tamogatas [29-39-0T147]; OTKA-PDOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [112118]; Janos Bolyai Research Scholarship of the Hungarian Academy of SciencesHungarian Academy of Sciences; A tehetseg ertekenek kibontakoztatasa a Szegedi Tudomanyegyetem kivalosaga erdekeben [TAMOP-4.2.2.B-15/1/KONV-2015-0006]; National Research, Development and Innovation Office grant [GINOP-2.3.2-15-2016-00020]; EU ITN aDDRess consortium [316390] Funding text: We thank Gabriella Pankotai-Bodo for discussion and revisions. We also thank Gyulane Okros for help with U2OS cells and Edina Pataki for technical assistance. This work was supported by Kutatoegyetemi es Kivalosagi EMMI tamogatas [29-39-0T147], OTKA-PD [112118], the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences and 'A tehetseg ertekenek kibontakoztatasa a Szegedi Tudomanyegyetem kivalosaga erdekeben' [TAMOP-4.2.2.B-15/1/KONV-2015-0006] and the National Research, Development and Innovation Office grant GINOP-2.3.2-15-2016-00020. A. Gy. was funded by EU ITN aDDRess consortium (GA number: 316390). Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, 6726, Hungary Department of Molecular Genetics, Erasmus University Medical Centre, Rotterdam, PO Box 2040CA 3000, Netherlands Institute of Biochemistry, Biological Research Centre, Szeged, 6726, Hungary Cited By :5 Export Date: 29 August 2020 Correspondence Address: Pankotai, T.; Department of Biochemistry and Molecular Biology, University of SzegedHungary; email: pankotai@bio.u-szeged.hu Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, 6726, Hungary Department of Molecular Genetics, Erasmus University Medical Centre, Rotterdam, PO Box 2040CA 3000, Netherlands Institute of Biochemistry, Biological Research Centre, Szeged, 6726, Hungary Cited By :5 Export Date: 30 August 2020 Correspondence Address: Pankotai, T.; Department of Biochemistry and Molecular Biology, University of SzegedHungary; email: pankotai@bio.u-szeged.hu Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, 6726, Hungary Department of Molecular Genetics, Erasmus University Medical Centre, Rotterdam, PO Box 2040CA 3000, Netherlands Institute of Biochemistry, Biological Research Centre, Szeged, 6726, Hungary Cited By :5 Export Date: 10 January 2021 Correspondence Address: Pankotai, T.; Department of Biochemistry and Molecular Biology, University of SzegedHungary; email: pankotai@bio.u-szeged.hu Funding details: Seventh Framework Programme, FP7, 316390 Funding details: Hungarian Scientific Research Fund, OTKA, 112118 Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, 6726, Hungary Department of Molecular Genetics, Erasmus University Medical Centre, Rotterdam, PO Box 2040CA 3000, Netherlands Institute of Biochemistry, Biological Research Centre, Szeged, 6726, Hungary Cited By :5 Export Date: 11 January 2021 Correspondence Address: Pankotai, T.; Department of Biochemistry and Molecular Biology, University of SzegedHungary; email: pankotai@bio.u-szeged.hu Funding details: Seventh Framework Programme, FP7, 316390 Funding details: Hungarian Scientific Research Fund, OTKA, 112118 Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, 6726, Hungary Department of Molecular Genetics, Erasmus University Medical Centre, Rotterdam, PO Box 2040CA 3000, Netherlands Institute of Biochemistry, Biological Research Centre, Szeged, 6726, Hungary Cited By :5 Export Date: 13 January 2021 Correspondence Address: Pankotai, T.; Department of Biochemistry and Molecular Biology, University of SzegedHungary; email: pankotai@bio.u-szeged.hu Funding details: Seventh Framework Programme, FP7, 316390 Funding details: Hungarian Scientific Research Fund, OTKA, 112118 Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, 6726, Hungary Department of Molecular Genetics, Erasmus University Medical Centre, Rotterdam, PO Box 2040CA 3000, Netherlands Institute of Biochemistry, Biological Research Centre, Szeged, 6726, Hungary Cited By :5 Export Date: 13 March 2021 Correspondence Address: Pankotai, T.; Department of Biochemistry and Molecular Biology, Hungary; email: pankotai@bio.u-szeged.hu Funding details: Seventh Framework Programme, FP7, 316390 Funding details: Hungarian Scientific Research Fund, OTKA, 112118 AB - The p53 tumour suppressor regulates the transcription initiation of selected genes by binding to specific DNA sequences at their promoters. Here we report a novel role of p53 in transcription elongation in human cells. Our data demonstrate that upon transcription elongation blockage, p53 is associated with genes that have not been reported as its direct targets. p53 could be co-immunoprecipitated with active forms of DNA-directed RNA polymerase II subunit 1 (RPB1), highlighting its association with the elongating RNA polymerase II. During a normal transcription cycle, p53 and RPB1 are localised at distinct regions of selected non-canonical p53 target genes and this pattern of localisation was changed upon blockage of transcription elongation. Additionally, transcription elongation blockage induced the proteasomal degradation of RPB1. Our results reveal a novel role of p53 in human cells during transcription elongation blockage that may facilitate the removal of RNA polymerase II from DNA. LA - English DB - MTMT ER - TY - JOUR AU - Szlávicz, Eszter AU - Szabó, Kornélia Ágnes AU - Groma, Gergely AU - Csörgő Sándorné Bata, Zsuzsanna AU - Pagani, F AU - Kemény, Lajos AU - Széll, Márta TI - Splicing factors differentially expressed in psoriasis alter mRNA maturation of disease-associated EDA+ fibronectin. JF - MOLECULAR AND CELLULAR BIOCHEMISTRY J2 - MOL CELL BIOCHEM VL - 436 PY - 2017 IS - 1-2 SP - 189 EP - 199 PG - 11 SN - 0300-8177 DO - 10.1007/s11010-017-3090-1 UR - https://m2.mtmt.hu/api/publication/3237714 ID - 3237714 AB - The EDA+ fibronectin splicing variant is overexpressed in psoriatic non-lesional epidermis and sensitizes keratinocytes to mitogenic signals. However, regulation of its abundance is only partially understood. In our recent cDNA microarray experiment, we identified three SR-rich splicing factors-splicing factor, arginine/serine-rich 18 (SFRS18), peptidyl-prolyl cis-trans isomerase G (PPIG), and luc-7 like protein 3 (LUC7L3)-which might be implicated in the preactivated states of keratinocytes in psoriatic non-involved skin and could also contribute to the regulation of fibronectin mRNA maturation. In this study, we investigated the role of LUC7L3, PPIG, and SFRS18 in psoriasis and in the mRNA maturation process of fibronectin. Regarding tissue staining experiments, we were able to demonstrate a characteristic distribution of the splicing factors in healthy, psoriatic non-involved and involved epidermis. Moreover, the expression profiles of these SR-rich proteins were found to be very similar in synchronized keratinocytes. Contribution of splicing facwwtors to the EDA+ fibronectin formation was also confirmed: their siRNA silencing leads to altered fibronectin mRNA and protein expression patterns, suggesting the participation in the EDA domain inclusion. Our results indicate that LUC7L3, PPIG, and SFRS18 are not only implicated in EDA+ fibronectin formation, but also that they could possess multiple roles in psoriasis-associated molecular abnormalities. LA - English DB - MTMT ER -