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Updated: Jun 15, 2026

Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions
Published on: September 28, 2017
Identification of protein interaction regions of VINC/NEAT1/Men epsilon RNA
U M Sreenivasa Murthy1, Pundi N Rangarajan
1Department of Biochemistry, Indian Institute of Science, Bangalore, India.
Abstract:
The virus inducible non-coding RNA (VINC) was detected initially in the brain of mice infected with Japanese encephalitis virus (JEV) and rabies virus. VINC is also known as NEAT1 or Men epsilon RNA. It is localized in the nuclear paraspeckles of several murine as well as human cell lines and is essential for paraspeckle formation. We demonstrate that VINC interacts with the paraspeckle protein, P54nrb through three different protein interaction regions (PIRs) one of which (PIR-1) is localized near the 5' end while the other two (PIR-2, PIR-3) are localized near the 3' region of VINC. Our studies suggest that VINC may interact with P54nrb through a novel mechanism which is different from that reported for protein coding RNAs.
Insights
Virus inducible non-coding RNA (VINC), also known as NEAT1, is essential for nuclear paraspeckle formation. This study reveals VINC interacts with P54nrb via novel mechanisms, distinct from protein-coding RNAs.
Area of Science:
- Molecular Biology
- Virology
- Genetics
Background:
- Virus inducible non-coding RNA (VINC), also known as NEAT1, is found in the brain during viral infections like Japanese encephalitis virus (JEV) and rabies virus.
- VINC is crucial for the formation of nuclear paraspeckles in both mouse and human cells.
Purpose of the Study:
- To investigate the interaction mechanism between VINC and the paraspeckle protein P54nrb.
- To identify the specific regions of VINC involved in binding to P54nrb.
Main Methods:
- Localization studies of VINC within nuclear paraspeckles.
- Protein-protein interaction assays to map VINC's binding sites for P54nrb.
Main Results:
- VINC interacts with P54nrb through three distinct protein interaction regions (PIRs).
- PIR-1 is located at the 5' end, while PIR-2 and PIR-3 are at the 3' region of VINC.
- The interaction mechanism between VINC and P54nrb appears novel and differs from known mechanisms for protein-coding RNAs.
Conclusions:
- VINC plays a significant role in nuclear paraspeckle structure and function.
- The identified interaction regions provide insights into the molecular basis of VINC-P54nrb binding.
- This study highlights a unique RNA-protein interaction mechanism relevant to non-coding RNAs.
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