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Published on: May 13, 2019
Pinning down transcription: regulation of RNA polymerase II activity during the cell cycle
1Department of Biological Sciences, Columbia University, New York, New York 10027, USA.
Abstract:
Pin1 is a peptidyl-prolyl cis/trans isomerase that was initially discovered as an important mitotic regulator. In keeping with this, it targets specifically phosphorylated ser- or thr-pro dipeptides, which are found in numerous mitotic proteins as a result of cyclin-dependent kinase activity. But Pin1 also modulates the activity of numerous other proteins, and a strong candidate for such regulation has been RNA polymerase II (RNAP II). The unique C-terminal domain of the RNAP II largest subunit contains as many as 100 ser-pro dipeptides laid out in an essentially linear array, and which are subject to different patterns of phosphorylation. Here we summarize findings indicating that Pin1 can indeed directly modulate the structure and function of RNAP II, and propose that this activity plays a role both in mitotic gene silencing and during the transcription cycle.
Insights
Pin1, a mitotic regulator, directly influences RNA polymerase II (RNAP II) function. This interaction is key for gene silencing during mitosis and the transcription cycle.
Area of Science:
- Molecular Biology
- Biochemistry
- Cell Biology
Background:
- Pin1 is a peptidyl-prolyl cis/trans isomerase regulating mitotic proteins.
- Pin1 targets phosphorylated ser- or thr-pro dipeptides, common in proteins phosphorylated by cyclin-dependent kinases.
- RNA polymerase II (RNAP II) is a potential target for Pin1 regulation due to its C-terminal domain structure.
Purpose of the Study:
- To investigate the direct modulation of RNA polymerase II (RNAP II) by Pin1.
- To elucidate the role of Pin1 in regulating RNAP II structure and function.
- To explore Pin1's involvement in mitotic gene silencing and the transcription cycle.
Main Methods:
- Summarizing existing research findings on Pin1 and RNAP II interaction.
- Analyzing the structural features of RNAP II's C-terminal domain, including ser-pro dipeptides and phosphorylation patterns.
- Reviewing evidence for Pin1's functional modulation of RNAP II.
Main Results:
- Pin1 directly modulates the structure and function of RNAP II.
- The C-terminal domain of RNAP II contains numerous ser-pro dipeptides susceptible to Pin1 activity.
- Evidence suggests Pin1's role in regulating RNAP II activity.
Conclusions:
- Pin1 directly interacts with and regulates RNA polymerase II (RNAP II).
- This interaction is significant for both mitotic gene silencing and the broader transcription cycle.
- Pin1's role extends beyond mitosis to fundamental transcriptional processes.
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