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Open Access Green as soon as Postprint is submitted to ZB.
Protein arginine methylation during lytic adenovirus infection.
Biochem. J. 383, 259-265 (2004)
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.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
adenovirus; E1B-AP5; L4-100 kDa; protein arginine methyltransferase; S-adenosyl-L-methionine
ISSN (print) / ISBN
0264-6021
e-ISSN
1470-8728
Journal
Biochemical Journal / Reviews
Quellenangaben
Volume: 383,
Issue: 2,
Pages: 259-265
Publisher
Portland Press
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Molecular Immunology (IMI)