Protein Phosphatase 1 (PP1) is one of the most ubiquitous phosphatases that are found in all eukaryotic cells. PP1 binds with more than 200 known regulatory proteins to determine its substrate specificity. Almost all PP1 interactors have the canonical RVxF motif, which is required to bind to the RVxF hydrophobic pocket on PP1, as well as additional PP1-interacting motifs to enhance binding. Ribosomal RNA processing 1 homolog B (RRP1B) targets PP1 to the nucleolus and is involved in the processing of the pre-60S ribosomal subunit. Since there are not many known nucleolar targeting proteins for PP1, characterizing the interaction between RRP1B and PP1 will help us to understand different targeting mechanisms and ultimately to unravel the PP1 code. Here we demonstrate that RRP1B shows strong differential binding for two isoforms of PP1, PP1 gamma and PP1 alpha, using Isothermal Titration Calorimetry. We also show that the RRP1B construct we used for this experiment is intrinsically disordered using 1H-15N-Heteronuclear Single Quantum Coherence spectroscopy.
Cho, Haejun, Bajaj, Rakhi, Ganesan, Senthill, et al.,
"Biophysical characterization of the RRP1B-PP1 holoenzyme"
(2016).
Summer Research Symposium.
Brown Digital Repository. Brown University Library.
https://doi.org/10.26300/872q-0z92
Each year, Brown University showcases the research of its undergraduates at the Summer Research Symposium. More than half of the student-researchers are UTRA recipients, while others receive funding from a variety of Brown-administered and national programs and fellowships and go …
