MYB elongation is regulated by the nucleic acid binding of NFκB p50 to the intronic stem-loop region

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. and Ramsay, Robert G. (2015) MYB elongation is regulated by the nucleic acid binding of NFκB p50 to the intronic stem-loop region. PLoS One, 10 4: 1-25. doi:10.1371/journal.pone.0122919


Author 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.
Title MYB elongation is regulated by the nucleic acid binding of NFκB p50 to the intronic stem-loop region
Formatted title
MYB elongation is regulated by the nucleic acid binding of NFκB p50 to the intronic stem-loop region
Journal name PLoS One   Check publisher's open access policy
ISSN 1932-6203
Publication date 2015-04-08
Year available 2015
Sub-type Article (original research)
DOI 10.1371/journal.pone.0122919
Open Access Status DOI
Volume 10
Issue 4
Start page 1
End page 25
Total pages 25
Place of publication San Francisco, CA United States
Publisher Public Library of Science
Collection year 2016
Language eng
Formatted 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.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
School of Pharmacy Publications
UQ Diamantina Institute Publications
 
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Citation counts: TR Web of Science Citation Count  Cited 1 times in Thomson Reuters Web of Science Article | Citations
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Created: Wed, 22 Apr 2015, 16:00:32 EST by Professor Tom Gonda on behalf of School of Pharmacy