FACULTY - SECONDARY FACULTY - DONNA M. DRISCOLL

Donna M. Driscoll, Ph.D.

Staff Scientist

Cell Biology Department
Lerner Research Institute, Cleveland Clinic

RNA Center Faculty:

since 2002

Education:

Ph.D.: Pathology
University of Chicago, 1984

Cleveland Clinic:

since 1992

Curriculum Vitae

Research:
Mechanisms of posttranscriptional gene regulation:
RNA editing and translational recoding of UGA as selenocysteine

Our research focuses on posttranscriptional mechanisms that expand the genetic diversity of the genome. The editing of apolipoprotein-B (apo-B) mRNA involves the site-specific deamination of cytidine to uridine, which converts a glutamine codon to an in-frame stop codon. Our goals are to determine how the editing enzyme recognizes apo-B mRNA, analyze the holoenzyme complex, and identify novel mRNA targets of the editing enzyme. The second project studies the translational recoding of UGA as selenocysteine (Sec), the 21rst amino acid. Ongoing projects are to identify the mRNA sequences and trans-acting factors required for Sec incorporation, and investigate how this pathway is regulated by selenium.

 

Selected Publications

Chavatte, L. and D.M. Driscoll (2005)
Ribosomal protein L30 is a component of the UGA/selenocysteine recoding machinery in eukaryotes.
Nature Str. Mol. Biol, 12, 408-416, 2005. /

Mehta, A. and D.M. Driscoll (2002)
Identification of domains in Apobec-1 Complementation Factor required for RNA binding and apolipoprotein-B mRNA editing.
RNA, 8: 69-82, 2002. /

Fletcher, J.E., Copeland, P.R., Driscoll, D.M., and A. Krol. (2001)
The selenocysteine incorporation machinery: Interactions between the SECIS RNA and SECIS-binding protein SBP2.
RNA, 7:1442-1453, 2001. /

Copeland, P.R., Stepanik, V.A., and D.M. Driscoll (2001)
Insight into mammalian selenocysteine insertion: Domain structure and ribosome binding properties of Sec insertion sequence binding protein-2.
Mol. Cell. Biol., 21:1491-1496, 2001. /