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Updated: Aug 23, 2026

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
Published on: December 16, 2021
Protein arginine methylation during lytic adenovirus infection
Julia Kzhyshkowska1, Elisabeth Kremmer, Markus Hofmann
1Institut für Medizinische Mikrobiologie und Hygiene, Universität Regensburg, Landshuterstr. 22, D-93053 Regensburg, Germany. julia.kzhyshkowska@haut.ma.uni-heidelberg.de
Abstract:
Arginine methylation of proteins affects major processes in the cell, including transcriptional regulation, mRNA metabolism, signal transduction and protein sorting. Arginine methylation of Ad (adenovirus) E1B 55-kDa-associated protein E1B-AP5 was recently described by us [Kzhyshkowska, Schutt, Liss, Kremmer, Stauber, Wolf and Dobner (2001) Biochem. J. 358, 305-314]. In this first example of protein arginine methylation analysis in Ad-infected cells, we investigated methylation of the E1B-AP5 and the viral L4-100 kDa protein. We demonstrate that E1B-AP5 methylation is enhanced during the course of infection in a cell-type-specific manner. We also show that L4-100 kDa is efficiently methylated in Ad-infected cells. L4-100 kDa formed complex with methyltransferase in vivo during productive infection, and can be methylated by HRMT1L2 (human protein arginine methyltransferase 1) in vitro. Comparative analysis of E1B-AP5 and L4-100 kDa protein methylation in Ad-infected HeLa, MCF-7 and H1299 cells revealed that the profile of protein arginine methylation correlates with the efficiency of Ad proteins production. Our results suggest that protein arginine methylation is an important host-cell function required for efficient Ad replication.
Insights
Protein arginine methylation is crucial for adenovirus replication. This study shows viral proteins like E1B-AP5 and L4-100 kDa are methylated, enhancing viral production in host cells.
Area of Science:
- Molecular Biology
- Virology
- Post-translational Modifications
Background:
- Protein arginine methylation is a key post-translational modification impacting cellular processes.
- Adenovirus (Ad) infection involves complex interactions with host cell machinery.
- Previous work identified arginine methylation of Ad E1B-associated protein E1B-AP5.
Purpose of the Study:
- To investigate protein arginine methylation in Ad-infected cells, focusing on E1B-AP5 and the viral L4-100 kDa protein.
- To determine the role of host cell protein arginine methylation in Ad replication efficiency.
- To analyze cell-type-specific methylation patterns of viral proteins.
Main Methods:
- Analysis of protein arginine methylation in Ad-infected human cell lines (HeLa, MCF-7, H1299).
- In vivo complex formation assays between viral proteins and methyltransferases.
- In vitro methylation assays using purified HRMT1L2 (human protein arginine methyltransferase 1).
Main Results:
- Arginine methylation of E1B-AP5 is enhanced during Ad infection in a cell-type-specific manner.
- The viral L4-100 kDa protein is efficiently methylated in Ad-infected cells and forms complexes with methyltransferases in vivo.
- L4-100 kDa can be methylated in vitro by HRMT1L2.
- Correlation observed between protein arginine methylation profiles and Ad protein production efficiency.
Conclusions:
- Protein arginine methylation of viral proteins is enhanced during adenovirus infection.
- Host cell protein arginine methylation appears to be essential for efficient adenovirus replication.
- Specific methyltransferases like HRMT1L2 may play a role in methylating viral proteins.
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