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Thomas Hollis, Ph.D.Wake Forest School of Medicine

Thomas Hollis, Ph.D.


Contact Information

Academic: 336-716-0768 | Department: 336-716-0768


Education & Training

  • B.S., Florida State University, 1992
  • Ph.D., University of Texas-Austin, 1997
  • Fellowship, Protein Biochemistry, Harvard Medical School, 2002


  • American Crystallographic Asso
  • Am Soc Of Biochem & Mol Biolog
Thomas Hollis, Ph.D.

Thomas Hollis, Ph.D.

Professor, Biochemistry

Research Interests

Exodeoxyribonucleases; Phosphoproteins; DNA; Models, Molecular; Ribonuclease H
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Contact Information

Academic: 336-716-0768 | Department: 336-716-0768


Recent Publications

Blocking LPA-dependent signaling increases ovarian cancer cell death in response to chemotherapy. Rogers LC, Davis RR, Said N, Hollis T, Daniel LW.. Redox Biol. 2018;15():380-386.

SAMHD1: recurring roles in cell cycle, viral restriction, cancer, and innate immunity. Mauney CH, Hollis T.. Autoimmunity. 2018;51(3):96-110.

The transcriptional regulator BpsR controls the growth of Bordetella bronchiseptica by repressing genes involved in nicotinic acid degradation. Guragain M, Jennings-Gee J, Cattelan N, Finger M, Conover MS, Hollis T, Deora R.. J Bacteriol. 2018;200(12):e00712-17.

The SAMHD1 dNTP triphosphohydrolase is controlled by a redox switch. Mauney CH, Rogers LC, Harris RS, Daniel LW, Devarie-Baez NO, Wu H, Furdui CM, Poole LB, Perrino FW, Hollis T.. Antioxid Redox Signal. 2017;27(16):1317-1331.

Solid-state nanopore analysis of diverse DNA base modifications using a modular enzymatic labeling process. Wang F, Zahid OK, Swain BE, Parsonage D, Hollis T, Harvey S, Perrino FW, Kohli RM, Taylor EW, Hall AR.. Nano Lett. 2017;17(11):7110-7116.

Crystal structure of RNA-DNA duplex provides insight into conformational changes induced by RNase H binding. Davis RR, Shaban NM, Perrino FW, Hollis T.. Cell Cycle. 2015;14(4):668-673.

Exonuclease TREX1 degrades double-stranded DNA to prevent spontaneous lupus-like inflammatory disease. Grieves JL, Fye JM, Harvey S, Grayson JM, Hollis T, Perrino FW.. Proc Natl Acad Sci U S A. 2015;112(16):5117-5122.

The Arg-62 residues of the TREX1 exonuclease act across the dimer interface contributing to catalysis in the opposing protomers. Fye JM, Coffin SR, Orebaugh CD, Hollis T, Perrino FW.. J Biol Chem. 2014;289(16):11556-65.

Cationic antimicrobial peptides promote microbial mutagenesis and pathoadaptation in chronic infections. Limoli DH, Rockel AB, Host KM, Jha A, Kopp BT, Hollis T, Wozniak DJ.. PLoS Pathog. 2014;10(4):e1004083.

The high-molecular-weight kininogen domain 5 is an intrinsically unstructured protein and its interaction with ferritin is metal mediated. Huhn AJ, Parsonage D, Horita DA, Torti FM, Torti SV, Hollis T.. Protein Sci. 2014;23(8):1013-1022.

The TREX1 C-terminal region controls cellular localization through ubiquitination. Orebaugh CD, Fye JM, Harvey S, Hollis T, Wilkinson JC, Perrino FW.. J Biol Chem. 2013;288(40):28881-92.

Defects in DNA degradation revealed in crystal structures of TREX1 exonuclease mutations linked to autoimmune disease. Bailey SL, Harvey S, Perrino FW, Hollis T.. DNA Repair. 2012;11(1):65-73.

The transcription factor AmrZ utilizes multiple DNA binding modes to recognize activator and repressor sequences of Pseudomonas aeruginosa virulence genes. Pryor EE Jr, Waligora EA, Xu B, Dellos-Nolan S, Wozniak DJ, Hollis T.. PLoS Pathog. 2012;8(4):e1002648.

Crystallization of Pseudomonas aeruginosa AmrZ protein: development of a comprehensive method for obtaining and optimization of protein-DNA crystals. Pryor EE Jr, Wozniak DJ, Hollis T.. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012;68(Pt 8):985-993.

Functional consequences of the RNase H2A subunit mutations that cause Aicardi-Goutieres syndrome. Coffin SR, Hollis T, Perrino FW.. J Biol Chem. 2011;286(19):16984-91.

Dominant mutations of the TREX1 exonuclease gene in lupus and Aicardi-Goutieres syndrome. Fye JM, Orebaugh CD, Coffin SR, Hollis T, Perrino FW.. J Biol Chem. 2011;286(37):32373-82.

The TREX1 exonuclease R114H mutation in Aicardi-Goutieres syndrome and lupus reveals dimeric structure requirements for DNA degradation activity. Orebaugh CD, Fye JM, Harvey S, Hollis T, Perrino FW.. J Biol Chem. 2011;286(46):40246-54.

Aicardi-Goutieres syndrome gene and HIV-1 restriction factor SAMHD1 is a dGTP-regulated deoxynucleotide triphosphohydrolase. Powell RD, Holland PJ, Hollis T, Perrino FW.. J Biol Chem. 2011;286(51):43596-600.

Structural and mutational analysis of Escherichia coli AlkB provides insight into substrate specificity and DNA damage searching. Holland PJ, Hollis T.. PLoS ONE. 2010;5(1):e8680.

The structure of the mammalian RNase H2 complex provides insight into RNA.NA hybrid processing to prevent immune dysfunction. Shaban NM, Harvey S, Perrino FW, Hollis T.. J Biol Chem. 2010;285(6):3617-3624.

AmrZ beta-sheet residues are essential for DNA binding and transcriptional control of Pseudomonas aeruginosa virulence genes. Waligora EA, Ramsey DM, Pryor EE Jr, Lu H, Hollis T, Sloan GP, Deora R, Wozniak DJ.. J Bacteriol. 2010;192(20):5390-5401.

Lesion bypass of N2-ethylguanine by human DNA polymerase Iota. Pence MG, Blans P, Zink CN, Hollis T, Fishbein JC, Perrino FW.. J Biol Chem. 2009;284(3):1732-1740.

Small molecule induction of MSH2-dependent cell death suggests a vital role of mismatch repair proteins in cell death. Vasilyeva A, Clodfelter JE, Rector B, Hollis T, Scarpinato KD, Salsbury FR Jr.. DNA Repair. 2009;8(1):103-113.

RNaseH2 mutants that cause Aicardi-Goutieres syndrome are active nucleases. Perrino FW, Harvey S, Shaban NM, Hollis T.. J Mol Med. 2009;87(1):25-30.

DNA binding induces active site conformational change in the human TREX2 3'-exonuclease. de Silva U, Perrino FW, Hollis T.. Nucleic Acids Res. 2009;37(7):2411-2417.

Mutations in the 3 '-5 ' DNA exonuclease TREX1 cause monogenic and complex forms of lupus erythematosus [abstract]. Lee-Kirsch M, Gong M, Chowdhury D, Senenko L, Engel K, De Silva U, Bailey SL, Harvey S, Hollis T, Perrino FW, et al.. Eur J Pediatr. 2008;167(3):365.

Cooperative DNA binding and communication across the dimer interface in the TREX2 3 '--> 5 '-exonuclease. Perrino FW, de Silva U, Harvey S, Pryor EE Jr, Cole DW, Hollis T.. J Biol Chem. 2008;283(31):21441-52.

The TREX1 double-stranded DNA degradation activity is defective in dominant mutations associated with autoimmune disease. Lehtinen DA, Harvey S, Mulcahy MJ, Hollis T, Perrino FW.. J Biol Chem. 2008;283(46):31649-56.

The crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partnering. de Silva U, Choudhury S, Bailey SL, Harvey S, Perrino FW, Hollis T.. J Biol Chem. 2007;282(14):10537-43.

Crystallization of protein-DNA complexes. Hollis T.. Methods Mol Biol. 2007;363():225-237.

Heterozygous mutations in TREX1 cause familial chilblain lupus and dominant Aicardi-Goutieres syndrome. Rice G, Newman WG, Dean J, Patrick T, Parmar R, Flintoff K, Robins P, Harvey S, Hollis T, Perrino FW, et al.. Am J Hum Genet. 2007;80(4):811-815.

A mutation in TREX1 that impairs susceptibility to granzyme A-mediated cell death underlies familial chilblain lupus. Lee-Kirsch MA, Chowdhury D, Harvey S, Gong M, Senenko L, Engel K, Pfeiffer C, Hollis T, Gahr M, Perrino FW, et al.. J Mol Med. 2007;85(5):531-537.

Structural basis for 3-methyladenine recognition and removal by a highly-specific DNA glycosylase: the crystal structure of TAG in complex with DNA [abstract]. Herrin A, Hollis T, Eichman BF.. J Biomol Struct Dyn. 2007;24(6):614.

DNA damage recognition and repair by 3-methyladenine DNA glycosylase I (TAG). Metz AH, Hollis T, Eichman BF.. EMBO J. 2007;26(9):2411-2420.

The molecular mechanism of DNA damage recognition by MutS homologs and its consequences for cell death response. Salsbury FR Jr, Clodfelter JE, Gentry MB, Hollis T, Scarpinato KD.. Nucleic Acids Res. 2006;34(8):2173-2185.

All Publications

For a listing of recent publications, refer to PubMed, a service provided by the National Library of Medicine.

For a list of earlier publications, visit the Carpenter Library Publication Search.

Professor, Biochemistry

Thomas Hollis, Ph.D.

Thomas Hollis, Ph.D.

Professor, Biochemistry

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