Phosphorylation Modulates Secondary Structure of Intrinsically Disordered Regions in RNA Polymerase II
Research by scientists at Pennsylvania State University has shed light on the phosphorylation patterns of the intrinsically disordered C-terminal domain (CTD) of RNA polymerase II. The findings suggest that phosphorylation can alter the secondary structure of the CTD, specifically in regions with tandem repeats of the consensus sequence YSPTSPS. This research has significant implications for understanding transcriptional regulation and cotranscriptional events.
Key Takeaways:
- The CTD of RNA polymerase II contains tandem repeats with the consensus sequence YSPTSPS, which are critical for transcriptional regulation.
- Phosphorylation of the CTD can modulate its secondary structure, with different patterns of phosphorylation affecting the formation of beta strands and beta turns.
- Small-angle X-ray scattering revealed no significant changes in the CTD's global dimensions even at high phosphorylation levels, contradicting the common assumption of phosphorylation-induced chain expansion.
- Ser2 phosphorylation can disrupt transient beta structures in early elongation, while Ser5 phosphorylation can restore them near termination for recruiting beta turn-recognizing termination factors.
- This research highlights the importance of understanding the dynamics of CTD structure and its regulation by phosphorylation in RNA polymerase II.
- The findings have significant implications for our understanding of transcriptional regulation and cotranscriptional events.
- The study's lead author, Scott A. Showalter, is affiliated with the Pennsylvania State University (Penn State) Department of Chemistry.
- Additional authors include Wei Chen, Tatiana N. Laremore, and Neela H. Yennawar.
Statistics:
- The research was supported by the National Science Foundation (NSF) and the Eberly Postdoctoral Research Fellowship.
- The study utilized X-ray scattering techniques to investigate the global dimensions of the CTD
- The researchers generated two distinct phosphorylation patterns: one with primarily Ser2 phosphorylation and another with hyperphosphorylation of Ser2, Ser5, and Thr residues.
- The study found that unphosphorylated CTD adopted transient beta strands at Ser2 during transcription preinitiation.
Sources:
- NewsRx. Data on DNA-Directed DNA Polymerase Discussed by Researchers at Pennsylvania State University (Penn State) (Phosphorylation Modulates Secondary Structure of Intrinsically Disorder Regions In Rna Polymerase Ii). Life Science Weekly. July 1, 2025; p 605.
- American Society for Biochemistry and Molecular Biology - www.asbmb.org
- Journal of Biological Chemistry - www.jbc.org
- Journal of Biological Chemistry, 2025;301(6), published by Elsevier.