Identification of NG-Methylarginine Residues in Human Heterogeneous RNP Protein A1: Phe/Gly-Gly-Gly-Arg-Gly-Gly-Gly/Phe Is a Preferred Recognition Motif
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- 作者：Sangduk Kim ; Barbara M. Merrill ; Ramesh Rajpurohit ; Amalendra Kumar ; Kathryn L. Stone ; Vladimir V. Papov ; Jennifer M. Schneiders ; Wlodzimierz Szer ; Samuel H. Wilson ; Woon Ki Paik ; and Kenneth R. Willi
- 刊名：Biochemistry
- 出版年：1997
- 出版时间：April 29, 1997
- 年：1997
- 卷：36
- 期：17
- 页码：5185 - 5192
- 全文大小：150K
- 年卷期：v.36,no.17(April 29, 1997)
- ISSN：1520-4995
文摘
Three sites ofNG,NG-argininemethylation have been located at residues 205, 217, and 224inthe glycine-rich, COOH-terminal one-third of the HeLa A1 heterogeneousribonucleoprotein. Togetherwith the previously determined dimethylated arginine at position 193[Williams et al., (1985) Proc. Natl.Acad. Sci. U.S.A. 82, 5666-5670], it isevident that all four sites fall within a span of sequencebetweenresidues 190 and 233 that contains multiple Arg-Gly-(Gly) sequencesinterspersed with phenylalanineresidues. These RGG boxes have been postulated to represent an RNAbinding motif [Kiledjian andDreyfuss (1992) EMBO J. 11, 2655-2664].Dimethylation of HeLa A1 appears to be quantitativeateach of the four positions. Arginines 205 and 224 have beenmethylated in vitro by a nuclear proteinarginine methyltransferase using recombinant (unmethylated) A1 assubstrate. This suggests A1 may bean in vivo substrate for this enzyme. Examination ofsequences surrounding the sites of methylation inA1 along with a compilation from the literature of sites that have beenidentified in other nuclear RNAbinding proteins suggests a methylase-preferred recognition sequence ofPhe/Gly-Gly-Gly-Arg-Gly-Gly-Gly/Phe, with the COOH-terminal flanking glycine being obligatory.Taken together with data in theliterature, identification of the sites of A1 arginine methylationstrongly suggests a role for this modificationin modulating the interaction of A1 with nucleic acids.