Tanya Paull

Paull, Tanya
Associate Professor in Molecular Genetics & Microbiology
Howard Hughes Medical Institute Investigator

E-mail: tpaull@mail.utexas.edu

Website: http://www.biosci.utexas.edu/mgm/People/Faculty/profiles/?id=1740

Main Office: MBB 2.212AA
Phone: 232-7802

Alternate Office: MBB 2.212
Phone: 232-7803

Mailing Address:
The University of Texas at Austin - ICMB
1 University Station A4800
2500 Speedway, MBB 2.212
Austin, TX 78712-1095


Research Summary:
   

Research in the lab is focused on the DNA damage response in eukaryotic cells, specifically the checkpoint activation and DNA repair responses that occur immediately after the introduction of chromosomal double-strand breaks. Several components of these DNA damage response systems have been implicated as tumor suppressors in mammalian organisms, thus establishing these factors as major targets in the progression from normal to unregulated cell growth.

Current studies in the lab are primarily focused on the biochemical activities of a complex of proteins, Mrell/Rad50/Nbs1 (M/R/N), which are critical components in the repair of DNA double-strand breaks. We study the activities of recombinant M/R/N complexes in vitro to characterize its functions on different types of DNA substrates and recombination intermediates. In addition, in vivo assays in S. cerevisiae are utilized to identify functions of the complex and the effects of mutant complexes in cells. Our overall goal is to decipher the functions of each of these factors at a molecular level in order to understand how they cooperate to guard cells against genetic rearrangements and transformation.


 
Research Images:


 
Publications:
Sae2 Is an Endonuclease that Processes Hairpin DNA Cooperatively with the Mre11/Rad50/Xrs2 Complex (2007) Molecular Cell 28, 638-651.
Rad50 Adenylate Kinase Activity Regulates DNA Tethering by Mre11/Rad50 complexes (2007) Molecular Cell 25, 647-661.
MDC1 maintains genomic stability by participating in the amplification of ATM- dependent DNA damage signals (2006) Mol Cell 21, 187-200.
The Mre11/Rad50/Xrs2 complex and non-homologous end-joining of incompatible ends in S. cerevisiae (2005) DNA Repair 4, 1281-1294.
ATM activation by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex (2005) Science 308, 551-554.
The rad50 signature motif: essential to ATP binding and biological function (2004) Journal of Molecular Biology 335, 937-51.
Direct Activation of the ATM protein kinase by the Mre11/Rad50/Nbs1 complex (2004) Science 304, 93-96.
Regulation of Mre11/Rad50 by Nbs1: effects on nucleotide-dependent DNA binding and association with ATLD mutant complexes (2003) Journal of Biological Chemistry 278, 45171-45181.

 
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