Monica Pillon
University at Buffalo, NY·Biochemistry
Mitochondria, the cell's energy producers, have their own ribosomes, the machines that make proteins. Building these ribosomes requires chemical edits to their RNA.
- Fields
Biochemistry
Biophysics
Genetics
- Topics
mitochondria
mitoribosome assembly
ribosomal RNA
- Grants
- 1 known grant, through Jun 2027
What they work on
- Determine how the RPUSD4 pseudouridine synthase, an RNA-editing enzyme, achieves strict specificity for its single modification site in mitochondrial ribosomal RNA, using structural biology and biochemistry.
- Define why mitochondrial disease mutations dysregulate the pseudouridine synthase module, combining biochemical and genomic approaches.
- Reveal how the pseudouridine synthase module recognizes assembling mitochondrial ribosomes, using hybrid structural biology.
More about the research
One such edit, pseudouridylation, converts the RNA letter uridine into a related form called pseudouridine. Faults in this editing have been linked to inherited mitochondrial diseases such as MELAS (mitochondrial encephalomyopathy, lactic acidosis and stroke-like episodes). How the editing enzymes pick the right site at the right time is unknown.
Why it matters
Patients with mitochondrial genetic disorders such as MELAS could benefit from knowing how faulty RNA-editing enzymes disrupt mitochondrial protein production. Explaining why disease mutations derail the RPUSD4 module could clarify disease mechanisms. It could also provide a framework for future approaches that target mitochondrial RNA processing.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Guillaume Chanfreau
University of California-Los Angeles, CA·Biochemistry
Determine how nuclear ribonucleases, including the RNA exosome, RNase III and the Rex exonucleases, regulate expression of chromatin remodeling factors such as bromodomain proteins when cells are placed under stress.
Emanuele Barca
Columbia University, NY·Medicine & Clinical Research·Early-career
Determine how defects in ATP synthase dimerization alter the shape of the inner mitochondrial membrane and disrupt the proton gradient, leading to ATP synthesis failure, using patient fibroblasts and knockout cell lines.
Daniel Dominguez
University of North Carolina at Chapel Hill, NC·Biochemistry
Define the mechanisms by which intrinsically disordered low-complexity domains (LCDs) of RNA binding proteins recognize structured RNA, such as RNA G-quadruplexes, using biochemical and computational approaches.
The school
University at Buffalo: 32 labs on PI Pages, $542M a year on research, 316 research doctorates a year.
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