Kzhyshkowska, Julia and Schuett, Holger and Liss, Michael and Kremmer, Elisabeth and Staubert, Roland and Wolf, Hans and Dobner, Thomas (2001) Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1. BIOCHEMICAL JOURNAL, 358. pp. 305-314. ISSN 0264-6021
Full text not available from this repository. (Request a copy)Abstract
The heterogeneous nuclear ribonucleoprotein (hnRNP) family includes predominantly nuclear proteins acting at different stages of mRNA metabolism. A characteristic feature of hnRNPs is to undergo post-translational asymmetric arginine methylation catalysed by different type 1 protein arginine methyltransferases (PRMTs). A novel mammalian hnRNP, E1B-AP5, recently identified by its interaction with adenovirus early protein E1B-55 kDa, has been proposed to have a regulatory role in adenoviral and host-cell mRNA processing/nuclear export [Gabler, Schutt, Groid, Wolf, Shenk and Dobner (1998) J. Virol. 72, 7960-7971]. Here we report that E1B-AP5 is methylated in vivo in its Arg-Gly-Gly (RGG)-box domain, known to mediate protein-RNA interactions. The activity responsible for E1B-AP5 methylation forms a complex with E1B-AP5 in vivo. The predominant mammalian arginine methyltransferase HRM1L2 (hPRMT1) did not detectably methylate endogenous E1B-AP5 despite efficiently methylating a recombinant RGG-box domain of E1B-AP5. Using yeast two-hybrid screening we identified HRMT1L1 (PRMT2) as one of the proteins interacting with E1B-AP5. By in situ immunofluorescence we demonstrated that E1B-AP5 co-localizes with the nuclear fraction of HRMT1L1. The Src homology 3 (SH3) domain of HRMT1L1 was essential for its interaction with E1B-AP5 in vivo. We suggest that HRMT1L1 is responsible for specific E1B-AP5 methylation in vivo.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | RNA-BINDING PROTEINS; NUCLEOCYTOPLASMIC TRANSPORT; N-METHYLTRANSFERASE; MOLECULAR-WEIGHT; TERMINAL DOMAIN; IN-VITRO; HNRNP-U; CELLS; EXPORT; A1; periodate-oxidized adenosine; S-adenosylmethionine; SH3 domain |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Medizinische Mikrobiologie und Hygiene |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 08 Dec 2021 15:16 |
| Last Modified: | 08 Dec 2021 15:16 |
| URI: | https://pred.uni-regensburg.de/id/eprint/41113 |
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