Protein arginine methylation during lytic adenovirus infection

Biochem J. 2004 Oct 15;383(Pt 2):259-65. doi: 10.1042/BJ20040210.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenoviridae / physiology*
  • Adenovirus E1B Proteins / metabolism*
  • Arginine / metabolism*
  • Cell Line, Tumor
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Methylation
  • Methyltransferases / metabolism
  • Organ Specificity
  • Protein-Arginine N-Methyltransferases
  • Time Factors
  • Viral Nonstructural Proteins / metabolism*
  • Virus Activation / physiology*

Substances

  • Adenovirus E1B Proteins
  • Intracellular Signaling Peptides and Proteins
  • L4-100K protein, adenovirus type 5
  • Viral Nonstructural Proteins
  • Arginine
  • Methyltransferases
  • PRMT2 protein, human
  • Protein-Arginine N-Methyltransferases