Air Lab  /  Bidichandani Lab  /  Broyles Lab /  DeAngelis Lab  / Hanas Lab  /  Levine Lab
Li Lab  /  Lin Lab  /  Matsumoto Lab  / Mooers Lab  /  Olson Lab  /  Rodgers Lab  /  Steinberg Lab
Weigel Lab  /  West Lab  /  Zlotnick Lab  /  Additional Graduate Students 

 Additional Departmental Employees

Structural biology of messenger RNA editing in the mitochondria of trypanosomes using X-ray crystallography and other physical technique to study RNA, RNA-binding proteins and their complexes.   

U-insertion/deletion editing in trypanosomes is a post-transcriptional process that corrects the coding sequence of most mitochondrial mRNAs.  This editing is required for the subsequent expression of several mitochondrial proteins. An enzyme cascade does the editing in the mitochondrion.  A RNA template directs the editing. 

However, unlike most other forms of information

transfer  between nucleic acids, this template is

divided  into   short   segments,  each  of  which

is embedded in a different species of non-coding

mitochondrial  RNA  termed  guide RNA (gRNA).

In some  cases,  over  half  of  the   final  coding

sequence  is  introduced  by  the  RNA   editing. 

This    extensive   editing    process  is  a  clear  

exception    to     the   central      paradigm    of 

molecular  biology  that  information   flows from 

DNA¦RNA¦protein.   The    evolutionary  basis 

for  such a  complex and  expensive  system  of

information flow is  still  unclear.    Our goal is to 

obtain  a  rigorous  description  of  the structural

biology of this type of RNA editing to improve our

understanding of its evolutionary basis and clarify

the relationship between this type of RNA editing

and other types of RNA editing.

Recent Publications:

Mooers, B. H. M.*  & Matthews, B. W.  (2006)  Extension to 2268 atoms of

direct methods in the ab initio determination of the unknown structure of bacteriophage P22 lysozyme. Acta Cryst. D 62, 165-76.  *Corresponding author.

Mooers, B. H. M., Logue, J. S. & Berglund, J. A. (2005)  The structural basis of myotonic dystrophy from the crystal structure of CUG repeats. Proc. Nat. Acad. Sci., USA 102, 16626-16631. 

Mooers, B. H. M. & Matthews, B. W. (2004) Use of an ion binding site to by-pass the 1000 atom limit to ab initio structure determination by direct methods. Acta Cryst. D 60, 1726-1737.

Sagermann, M. Gay, L., Mooers, B. H. M., & Matthews, B. W.  (2004)  Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding. Biochemistry 33, 1296-301.

Mooers, B. H. M., Datta, D., Zollars, E., Mayo, S. L., & Matthews, B. W. (2003) Repacking the core of T4 lysozyme by automated design. J. Mol. Biol.  332, 741-756.

Eichman, B. F., Mooers, B. H. M., Alberti, M., Hearst, J. E., & Ho, P. S. (2001) The crystal structures of psoralen cross-linked DNAs: Drug dependent formation of Holliday junctions. J. Mol. Biol. 308, 15-26.

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