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Phyllis
R. Strauss
Matthews
Distinguished Professor of Biology
Ph.D., The Rockefeller University
Research
Areas:
Cell Biology and Biochemistry
Publications
Email: p.strauss@neu.edu
Phone:
617.373.3492
Fax: 617.373.2138
Location:
106 Lake Hall
Mail: NU/Biology
134 Mugar Life Sciences
360 Huntington Avenue
Boston, MA 02115
USA
Research Description
My laboratory is interested in the relationship of DNA repair to cell physiology and carcinogenesis. We study the process of DNA repair by cloning the genes of specific enzymes involved in the repair of oxidative damage of DNA and base excision repair, expressing the proteins in a heterologous system and characterizing their function. We focus on human apurinic endonuclease (AP endo). The availability of large quantities of the enzyme make detailed structure/function studies possible.
Currently we are exploring a novel mechanism of catalysis in which a tyrosine in the active site is the residue that cleaves the DNA backbone 5' to the abasic site. We also use the zebrafish as a model organism to study the role of AP endo in develpment. All of these studies are aimed at understanding the physiological relevance of a key enzyme that participates in repair of oxidatively damaged DNA.
Selected
Publications
Melo, L., Mundle, S., Fattal, M., O’Regan, N.O. and Strauss, P.R. 2006 Role of active site tyrosines in dynamic aspects of DNA binding by AP endonuclease DNA Repair In press
Wang, Y., Shupenko, C.C., Melo, L.F. and Strauss, P.R. 2006 A DNA repair protein involved in heart and blood development Molecular Cell Biology 26, 9083-9093. PDF
Mundle,
S.T., Fattal, M.H., Melo, L.F., Coriolan, J.D. and Strauss,
P.R. 2004. Novel role of tyrosine in catalysis by human AP endonuclease
1. DNA Repair 3, 1447-1455. PDF
Mckenzie, A.J. and Strauss, P.R. 2003. A quantitative method for measuring protein phosphorylation Analyt. Biochem. 313, 9-16. PDF
Kolaczkowski, S.V., Perry, A., Mckenzie, A., Johnson, F., Budil, D.E. and Strauss, P.R. 2001. A spin-labeled abasic DNA substrate for AP endonuclease. Biochem. Biophys. Res. Commun.. 288, 722-726. PDF
Mckenzie, A.J. and Strauss, P.R. 2001. Oligonucleotides with bistranded abasic sites interfere with substrate binding and catalysis by human apurinic/apyrimidinic endonuclease. Biochemistry 40, 13254-13261. PDF
Wiesel, P., Foster,
L.C., Pellacani, A., Layne, M.D., Hsieh, C.-M., Huggins, G.S., Strauss,
P.R., Yet, S.-F. and Perrella, M.A. 2000. Thioredoxin facilitates the
induction of heme oxygenase 1 in response to inflammatory mediators. J.
Biol. Chem. 275, 4840-4846.
Budil, D.E., Kolaczkowski, S.V., Perry, A., Varaprasad, C., Johnson, F.
and Strauss, P.R. 1999. Anisotropic dynamics and local
ordering in a spin-labeled oligon
ucleotide observed by 220 GHz EPR spectroscopy. Biophys. J. 78, 430-438.
Carey, D. and Strauss, P.R. 1999. Human apurinic/apyrimidinic endonuclease is processive. Biochemistry 38, 16553-16560. PDF
Lucas,
J.A., Masuda, Y., Bennett, R.A.O., Strauss, N.S. and Strauss,
P.R. 1999. Single turnover analysis of mutant human apurinic/apyrimidinic
endonuclease. Biochemistry 38, 4958-4964. PDF
Prasad, R., Beard,
W.A., Strauss, P.R. and Wilson, S.H. 1998. Human DNA
polymerase ß deoxyribose phosphate lyase: substrate specificity
and catalytic mechanism. J. Biol. Chem. 273: 15263-15270.
Strauss,
P. R. and Holt, C. M. 1998. Domain mapping of human apurinic/apyrimidinic
endonuclease: Structural and functional evidence for a disordered amino
terminus and a tight globular carboxyl domain. J. Biol. Chem. 273: 14435-14441.
PDF
Strauss, P. R., Beard, W., Patterson, T.A. and Wilson, S. H. 1997. Substrate binding by human apurinic/apyrimidinic endonuclease indicates a Briggs-Haldane mechanism. J. Biol. Chem. 272: 1302-1307. PDF
Chyan, J., Strauss, P. R., Wood, T. and Wilson, S. 1996. Identification of novel mRNA isoforms for human DNA polymerase ß. DNA and Cell Biology 15: 653-659.
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