In Vivo Methylation of an Arginine in Chicken Myelin Basic Protein

Abstract

The amino acid sequence around the sole methylarginine residue in chicken myelin basic protein was determined and was found to be similar to that previously reported for mammalian myelin basic protein. The ratio NG, N'G-dimethylarginine: NG-monomethylarginine:arginine was approximately 1.3:0.9:1.0. No NG, NG-dimethylarginine was detected in the protein. The in vivo incorporation of methyl groups from [methyl-3H]methionine into methylarginines in myelin was found to occur readily in 2-day-old chickens. Radioactively labelled NG,N'G-dimethylarginine and NG-monomethylarginine in myelin were derived solely from myelin basic protein. Radioactivity was also incorporated into NG,NG-dimethylargnine, although this was not derived from myelin basic protein. As NG-monomethylarginine was easily separated from the dimethylarginines, and as it was derived from myelin basic protein, it may be a good marker for myelin basic protein turnover in vivo. A time course study of the incorporation showed that radioactivity was incorporated into NG-monomethylarginine up to 6 h after injection, and decayed slowly, with an apparent half-life of about 40 days.

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

“…3, Table 1) has been observed to be either unmodified, monomethylated, or dimethylated (Baldwin and Carnegie, 1971a,b;Jones and Carnegie, 1974;Small and Carnegie, 1982;Ghosh et al, 1991;Rawal et al, 1992;Gary and Clarke, 1998;Pritzker et al, 2000b). The dimethylated arginyl form is symmetric, a variant found only in one other kind of protein-SmD1 and SmD3 of small nuclear ribonucleoproteins involved in mRNA splicing (Brahms et al, 2000Meister et al, 2001).…”

Biological methylation of myelin basic protein: Enzymology and biological significance

“…In 1971, the occurrence of methylarginine at Res-107 of myelin basic protein (MBP) was reported independently by two groups of investigators (Baldwin and Carnegie, 1971;Brostoff and Eylar, 1971). Since this initial discovery, several laboratories have studied the MBP-arginine methylation in conjunction with myelination Kim, 1972, 1973;Jones methylation: (1) the molecular distinction and Carnegie, 1974;Small and Carnegie, 1982; between subclasses of PMI; and (2) the Crang and Jacobson, 1982). Since MBP is the biochemical significance of MBP-specific methmajor constituent of the myelin membrane ylation in relation to myelination in the central (Campagnoni,19X8) The enzyme (AdoMet: protein-arginine Nmethyltransferase) was initially discovered from calf thymus in 1968 (Paik and Kim, 1968) and the reaction yields three methylated arginine derivatives (Nakajima PZ al., 1971):…”

Developmental accumulation and heterogeneity of myelin basic protein transcripts in the chick visual system

“…As in mammals, the avian CNS may contain multiple forms of MBP, although earlier studies have described only one form of this protein in chicken (Franz et al, 1981;Martenson and Deibler, 1975;Small and Carnegie, 1982). Since most of the isolated cDNAs encode the 18.7K MBP and in S1 mapping experiments the majority of labelled fragments was completely protected from degradation (Fig.…”