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Phoebe Rice

Professor, Biochemistry & Molecular Biophysics

Education:

B.A., Biochemistry Brandeis University, 1986

Ph.D., Molecular Biophysics and Biochemistry Yale University, 1992

Post-doctoral fellow at LMB/NIDDK/NIH 1993-1997

Lab Members:

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Contact Information:

Email:

Office:
929 E. 57th Street
Chicago, IL 60637
GCIS
Phone: (773) 834-1723
Fax: (773) 702-0439

Lab:
929 E. 57th Street
Chicago, IL 60637
GCIS W125
Phone: (773) 834-1725

Phoebe A Rice

Research Summary / Selected Publications

We combine biochemistry and x-ray crystallography to study protein-DNA interactions and DNA recombination.
Site-specific DNA recombinases: These cut and paste DNA at defined sequences, and are useful genetic tools. They exchange DNA partners via a remarkable molecular swivel. Two favorites are:
(1) Sin, which aids stable maintenance of multi-resistance plasmids of S. aureus. Sin is regulated by the global topology of its plasmid substrate. In collaboration with the Stark group in Glasgow, we are using kinetics, crystallography, and molecular modeling to understand this enzyme at the molecular level.
(2) CcrA/B/C, which mobilize the methicillin-resistance encoding element that turns garden-variety S. aureus into MRSA. Their catalytic domain is related to Sin’s, but their regulation is very different and rather mysterious. This is a local collaboration with Drs. Daum and Boyle- Vavra, who study the epidemiology of MRSA.
“classical” DNA transposases: members of this family are closely related to retroviral integrases. They catalyze the mobility of numerous DNA transposons, contributing to horizontal gene transfer and antibiotic resistance in bacteria.
Rad51 and its prokaryotic counterpart...

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Boocock MR, Rice PA. A proposed mechanism for IS607-family serine transposases. Mob DNA. 2013 Nov 6;4(1):24.  

Misiura A, Pigli YZ, Boyle-Vavra S, Daum RS, Boocock MR, Rice PA. Roles of two large serine recombinases in mobilizing the methicillin-resistance cassette SCCmec. Mol Microbiol. 88(6):1218-29. (2013) 

Montaño, SP, Pigli, YZ, and Rice, PA. Structure of the Mu transpososome illuminates evolution of DDE recombinases. Nature, Nov 15;491(7424):413-7. (2012)  

Keenholtz RA, Mouw KW, Boocock MR, Li NS, Piccirilli JA, Rice PA. Arginine as a general acid catalyst in serine recombinase - mediated DNA cleavage. J Biol Chem. 2013 Aug 22. 

Keenholtz RA, Rowland SJ, Boocock MR, Stark WM, Rice PA. Structural basis for catalytic activation of a serine recombinase. Structure 19:799-809 (2011).  

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