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Deciphering the phosphorylation pattern of RNA polymerase II for eukaryotic transcription

Award Number: R35GM148356
ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
OPDIV: NIH
AWARD CLASS: DISCRETIONARY
AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)
PERIOD OF PERFORMANCE START DATE: 02/06/2023
PERIOD OF PERFORMANCE END DATE: 01/31/2028

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Deciphering the phosphorylation pattern of RNA polymerase II for eukaryotic transcription - ABSTRACT The C-terminal domain (CTD) of the largest RNA polymerase II subunit is a unique CTD sequence (Y1S2P3T4S5P6S7) repeated many times and is mostly conserved in eukaryotes. This domain coordinates the recruitment of transcriptional factors to Pol II through its post-translational modifications, the loss of which cripples the highly efficient transcription process and causes the cell to die. The accurate phosphorylation state of different residues in the CTD heptad repeats by kinase and phosphatases is crucial to precisely recruiting proteins to mediate the transcription process. Our lab utilizes our extensive experience in protein chemistry to understand the precise pattern of phosphorylation during transcription by investigating the activity and specificity of these kinases and phosphatases. We seek to understand how the post-translational modifications of CTD are altered during biological events and how such changes are reflected in the outcome of transcription. We use multi-disciplinary methods including structural biology, biochemistry, mass spectrometry methodology, and global transcriptome analysis to investigate the molecular mechanism of how different modification states of RNA polymerase II coordinate the eukaryotic transcription. Equipped with extensive knowledge about the phosphatase function and activity, we further explore how the chemical inhibition of SCP1, a human phosphatase belonging to HAD superfamily, thwarts some of the growth glioblastoma cells. We utilized our experience in structural-based inhibitor design to identify covalent and non- covalent inhibitors targeting this unique phosphatase.


Issue Date FY	Funding FY	Legal Entity Name	Legal Entity Address	Legal Entity City	Legal Entity State	Legal Entity Zip Code	Legal Entity COUNTY	Legal Entity COUNTRY	Assistance Listing	Award Code	Budget Year	Action Date	Action Type	Action Amount

Issue Date FY: 2025 ( Subtotal = $537,773 )
2025	2025	UNIVERSITY OF TEXAS AT AUSTIN	110 INNER CAMPUS DR	AUSTIN	TX	78712	TRAVIS	USA	Biomedical Research and Research Training	001	3	1/14/2025	NON-COMPETING CONTINUATION	$537,773
2025	2024	UNIVERSITY OF TEXAS AT AUSTIN	110 INNER CAMPUS DR	AUSTIN	TX	78712	TRAVIS	USA	Biomedical Research and Research Training	000	2	11/11/2024	NON-COMPETING CONTINUATION	$0
														Subtotal = $537,773

Issue Date FY: 2024 ( Subtotal = $597,526 )
2024	2024	UNIVERSITY OF TEXAS AT AUSTIN	110 INNER CAMPUS DR	AUSTIN	TX	78712	TRAVIS	USA	Biomedical Research and Research Training	000	2	1/16/2024	NON-COMPETING CONTINUATION	$537,773
2024	2024	UNIVERSITY OF TEXAS AT AUSTIN	110 INNER CAMPUS DR	AUSTIN	TX	78712	TRAVIS	USA	Biomedical Research and Research Training	001	2	6/21/2024	NON-COMPETING CONTINUATION	$59,753
														Subtotal = $597,526

Issue Date FY: 2023 ( Subtotal = $489,218 )
2023	2023	UNIVERSITY OF TEXAS AT AUSTIN	110 INNER CAMPUS DR	AUSTIN	TX	78712	TRAVIS	USA	Biomedical Research and Research Training	000	1	2/6/2023	NEW	$489,218
														Subtotal = $489,218

Grand Total All Awards = $1,624,517

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Deciphering the phosphorylation pattern of RNA polymerase II for eukaryotic transcription

Award Number: R35GM148356

ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES

OPDIV: NIH

AWARD CLASS: DISCRETIONARY

AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)

PERIOD OF PERFORMANCE START DATE: 02/06/2023

PERIOD OF PERFORMANCE END DATE: 01/31/2028

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