Authors

Kip Guja

Type

Text

Type

Dissertation

Advisor

Allaire, Marc | Garcia-Diaz, Miguel | Bogenhagen, Daniel | Karzai, A Wali | Glynn, Steven.

Date

2015-12-01

Keywords

Crystallography, Gene Expression, Mitochondria, MTERF, Structure, TFB1M | Biology

Department

Department of Biochemistry and Structural Biology.

Language

en_US

Source

This work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree.

Identifier

http://hdl.handle.net/11401/76954

Publisher

The Graduate School, Stony Brook University: Stony Brook, NY.

Format

application/pdf

Abstract

Mitochondria are dual membrane-bound organelles found in the cytoplasm of all eukaryotic cells. Human mitochondria contain a 16.5 kb double-stranded DNA genome that encodes thirteen essential protein subunits of the oxidative phosphorylation system, as well as the two ribosomal RNAs and 22 transfer RNAs needed to translate the thirteen messenger RNAs. Oxidative phosphorylation produces the majority of energy needed for cells to sustain life, and this process is strictly dependent on expression of the mitochondrial genome. Defects in mitochondrial gene expression are linked to many human diseases, age-related pathologies, and the aging process itself. Obtaining a more detailed understanding of the mechanisms of mitochondrial gene expression and their regulation by nuclear encoded proteins is a critical first step towards improving our ability to treat mitochondrial diseases and mitochondrial related pathologies. I have utilized structural biology techniques (mainly X-ray crystallography), complemented with biochemical and genetic experiments to gain novel insights into several key points of regulation, including ribosomal RNA modification, ribosome biogenesis, and termination of transcription. I have obtained novel X-ray crystallographic structures of an essential mitochondrial ribosomal RNA methyltransferase TFB1M, which has isoforms that are linked to maternally inherited deafness and increased risk for developing type II diabetes mellitus. I have demonstrated the methyltransferase activity of TFB1M using an in vivo complementation assay, and obtained a structure of TFB1M bound to the cofactor S- adenosylmethione, which reveals the structural basis for its activity. I have also obtained novel crystal structures of MTERF family proteins that regulate ribosome assembly and transcription termination in mitochondria, and also modulate pathogenesis of several diseases arising from mutations in the mitochondrial DNA. In sum, my results provide novel structural insights into several members of the mitochondrial gene expression machinery, suggest close links between regulation of transcription and RNA modification in mitochondria, and improve our understanding of the pathogenesis of mitochondrial disease. | 118 pages

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