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Title: MYB Elongation Is Regulated by the Nucleic Acid Binding of NFκB p50 to the Intronic Stem-Loop Region.
Austin Authors: Pereira, Lloyd A;Hugo, Honor J;Malaterre, Jordane;Huiling, Xu;Sonza, Secondo;Cures, Alina;Purcell, Damian F J;Ramsland, Paul A ;Gerondakis, Steven;Gonda, Thomas J;Ramsay, Robert G
Affiliation: Sir Peter MacCallum Department of Oncology, The University of Melbourne, Parkville, Victoria, 3010, Australia
Victorian Breast Cancer Consortium, Invasion and Metastasis Unit, St Vincent's Institute of Medical Research, Melbourne, Victoria, 3065, Australia
School of Pharmacy University of Queensland, Woolloongabba, Queensland, 4102, Australia
Australian Centre for Blood Diseases, Monash University, Prahran, Victoria 3004, Australia
The Department of Pathology, The University of Melbourne, Parkville, Victoria, 3010, Australia
Centre for Immunology, Burnet Institute, Melbourne, Victoria, 3004, Australia
Department of Surgery (Austin Health), The University of Melbourne, Heidelberg, Victoria, 3084, Australia
Differentiation and Transcription Laboratory, Peter MacCallum Cancer Centre, Locked Bag #1, Melbourne, Victoria, 8006, Australia
The Department of Microbiology and Immunology, The University of Melbourne, Parkville, Victoria, 3010, Australia
Department of Immunology, Monash University, Alfred Medical Research and Education Precinct, Melbourne, Victoria, 3004, Australia
Issue Date: 8-Apr-2015
Publication information: PLoS One 2015; 10(4): e0122919
Abstract: MYB transcriptional elongation is regulated by an attenuator sequence within intron 1 that has been proposed to encode a RNA stem loop (SLR) followed by a polyU tract. We report that NFκBp50 can bind the SLR polyU RNA and promote MYB transcriptional elongation together with NFκBp65. We identified a conserved lysine-rich motif within the Rel homology domain (RHD) of NFκBp50, mutation of which abrogated the interaction of NFκBp50 with the SLR polyU and impaired NFκBp50 mediated MYB elongation. We observed that the TAR RNA-binding region of Tat is homologous to the NFκBp50 RHD lysine-rich motif, a finding consistent with HIV Tat acting as an effector of MYB transcriptional elongation in an SLR dependent manner. Furthermore, we identify the DNA binding activity of NFκBp50 as a key component required for the SLR polyU mediated regulation of MYB. Collectively these results suggest that the MYB SLR polyU provides a platform for proteins to regulate MYB and reveals novel nucleic acid binding properties of NFκBp50 required for MYB regulation.
Gov't Doc #: 25853889
DOI: 10.1371/journal.pone.0122919
Type: Journal Article
Appears in Collections:Journal articles

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