Daniel Dominguez
University of North Carolina at Chapel Hill, NC·Biochemistry
Proteins that bind RNA, the working copy of a gene, control nearly every step of how genes are expressed: how messages are cut, moved, kept stable or destroyed. The textbook picture is that neatly folded protein pockets grab flexible strands of RNA.
- Fields
Biochemistry
Genetics
Biology
- Topics
RNA binding proteins
intrinsically disordered proteins
low-complexity domains
- Grants
- 1 known grant, through Apr 2031
What they work on
- 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.
- Determine the functional consequences of LCD–RNA interactions for RNA processing and gene regulation, using molecular biology methods and relevant animal models.
- Test how disease-causing mutations within RNA binding proteins change their RNA binding and regulatory function, and how this relates to developmental disorders.
- Examine how LCD function and protein isoform diversity differ across tissues and reshape RNA regulatory networks.
More about the research
Newer evidence suggests the reverse also happens. Floppy, unstructured stretches of protein, called intrinsically disordered low-complexity domains (LCDs), can recognize RNA that is itself tightly folded into shapes such as RNA G-quadruplexes (rG4s), four-stranded knots formed by guanine-rich sequences. How this works, and what goes wrong when these proteins are mutated in disease, is poorly understood.
Why it matters
Mutations in RNA binding proteins are tied to developmental disorders, but how they disrupt gene regulation is unclear. By defining how disordered protein regions recognize RNA, and how disease mutations alter this, the work could explain the molecular basis of RBP-linked developmental disorders and point to the pathways involved.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Steven L Mcknight
University of Texas Southwestern Medical Center, TX·Biochemistry
Identify and map thousands of distinct labile cross-beta cores, the short segments that nucleate self-association, within low-complexity domains across the human proteome using high-throughput methods.
Adam Norris
University of California-Riverside, CA·Genetics
Determine how the broadly expressed RNA binding protein MEC-8/RBPMS produces cell-specific outcomes by identifying its physiologically relevant RNA targets in different C. elegans cell and tissue types.
Shahar Sukenik
Syracuse University, NY·Biophysics
Determine when the structural preferences of disordered regions in transcription factors affect their function, by linking ensemble structure to transcriptional activity in live cells.
The school
University of North Carolina at Chapel Hill: 72 labs on PI Pages, $1.6B a year on research, 523 research doctorates a year.
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