title: Protein arginine methylation during lytic adenovirus infection.
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.
authors.affiliation: Institut für Medizinische Mikrobiologie und Hygiene, Universität Regensburg, Landshuterstr. 22, D-93053 Regensburg, Germany. julia.kzhyshkowska@haut.ma.uni-heidelberg.de
authors.forename: Julia
authors.initials: J
authors.lastname: Kzhyshkowska
authors.forename: Elisabeth
authors.initials: E
authors.lastname: Kremmer
authors.forename: Markus
authors.initials: M
authors.lastname: Hofmann
authors.forename: Hans
authors.initials: H
authors.lastname: Wolf
authors.forename: Thomas
authors.initials: T
authors.lastname: Dobner
mesh_terms: D000256:Adenoviridae / Q000502:physiology*; D017501:Adenovirus E1B Proteins / Q000378:metabolism*; D001120:Arginine / Q000378:metabolism*; D045744:Cell Line, Tumor; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism; D009928:Organ Specificity; D011484:Protein-Arginine N-Methyltransferases; D013997:Time Factors; D017361:Viral Nonstructural Proteins / Q000378:metabolism*; D014775:Virus Activation / Q000502:physiology*
chemical_list: D017501:Adenovirus E1B Proteins; D047908:Intracellular Signaling Peptides and Proteins; C477284:L4-100K protein, adenovirus type 5; D017361:Viral Nonstructural Proteins; D001120:Arginine; D008780:Methyltransferases; C077013:PRMT2 protein, human; D011484:Protein-Arginine N-Methyltransferases