Biochemical analysis of the arginine methylation of high molecular weight fibroblast growth factor-2

Sharon Klein; James A. Carroll; Yan Chen; Michael F. Henry; Pamela A. Henry; Izabela E. Ortonowski; Giuseppe Pintucci; Ronald C. Beavis; Wilson H. Burgess; Daniel B. Rifkin

doi:10.1074/jbc.275.5.3150

Biochemical analysis of the arginine methylation of high molecular weight fibroblast growth factor-2

Sharon Klein, James A. Carroll, Yan Chen, Michael F. Henry, Pamela A. Henry, Izabela E. Ortonowski, Giuseppe Pintucci, Ronald C. Beavis, Wilson H. Burgess, Daniel B. Rifkin

Molecular Biology

Rowan University

Research output: Contribution to journal › Article › peer-review

44 Scopus citations

Abstract

The post-translational methylation of the N-terminally extended or high molecular weight (HMW) forms of fibroblast growth factor-2 (FGF-2) has been shown to affect the nuclear accumulation of the growth factor. In this study, we determined the extent and position of methyl groups in HMW FGF-2. Using mass spectrometry and amino acid sequence analysis, we have shown that the 22- and 22.5-κDa forms of HMW FGF-2 contain five dimethylated arginines located at positions -22, -24, -26, -36, and -38 using the methionine residue normally used to initiate the 18-κDa form as position 0. The 24-κDa form of HMW FGF-2 contains seven to eight dimethylated arginines located at positions -48, -50, and -52, in addition to positions -22, -24, -26, -36, and -38. In vitro methylation reactions demonstrate that the N-terminal extension of HMW FGF-2 acts as a specific substrate for yeast Hmt1p and human HRMT1L2 arginine methyltransferases. These findings indicate that HMW FGF-2, with the presence of five or more dimethylated Gly-Arg-Gly repeats, contains an RGG box-like domain, which may be important for protein-protein and/or protein-RNA interactions.

Original language	American English
Pages (from-to)	3150-3157
Number of pages	8
Journal	Journal of Biological Chemistry
Volume	275
Issue number	5
DOIs	https://doi.org/10.1074/jbc.275.5.3150
State	Published - Feb 4 2000

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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title = "Biochemical analysis of the arginine methylation of high molecular weight fibroblast growth factor-2",

abstract = "The post-translational methylation of the N-terminally extended or high molecular weight (HMW) forms of fibroblast growth factor-2 (FGF-2) has been shown to affect the nuclear accumulation of the growth factor. In this study, we determined the extent and position of methyl groups in HMW FGF-2. Using mass spectrometry and amino acid sequence analysis, we have shown that the 22- and 22.5-κDa forms of HMW FGF-2 contain five dimethylated arginines located at positions -22, -24, -26, -36, and -38 using the methionine residue normally used to initiate the 18-κDa form as position 0. The 24-κDa form of HMW FGF-2 contains seven to eight dimethylated arginines located at positions -48, -50, and -52, in addition to positions -22, -24, -26, -36, and -38. In vitro methylation reactions demonstrate that the N-terminal extension of HMW FGF-2 acts as a specific substrate for yeast Hmt1p and human HRMT1L2 arginine methyltransferases. These findings indicate that HMW FGF-2, with the presence of five or more dimethylated Gly-Arg-Gly repeats, contains an RGG box-like domain, which may be important for protein-protein and/or protein-RNA interactions.",

author = "Sharon Klein and Carroll, \{James A.\} and Yan Chen and Henry, \{Michael F.\} and Henry, \{Pamela A.\} and Ortonowski, \{Izabela E.\} and Giuseppe Pintucci and Beavis, \{Ronald C.\} and Burgess, \{Wilson H.\} and Rifkin, \{Daniel B.\}",

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AU - Klein, Sharon

AU - Carroll, James A.

AU - Chen, Yan

AU - Henry, Michael F.

AU - Henry, Pamela A.

AU - Ortonowski, Izabela E.

AU - Pintucci, Giuseppe

AU - Beavis, Ronald C.

AU - Burgess, Wilson H.

AU - Rifkin, Daniel B.

PY - 2000/2/4

Y1 - 2000/2/4

N2 - The post-translational methylation of the N-terminally extended or high molecular weight (HMW) forms of fibroblast growth factor-2 (FGF-2) has been shown to affect the nuclear accumulation of the growth factor. In this study, we determined the extent and position of methyl groups in HMW FGF-2. Using mass spectrometry and amino acid sequence analysis, we have shown that the 22- and 22.5-κDa forms of HMW FGF-2 contain five dimethylated arginines located at positions -22, -24, -26, -36, and -38 using the methionine residue normally used to initiate the 18-κDa form as position 0. The 24-κDa form of HMW FGF-2 contains seven to eight dimethylated arginines located at positions -48, -50, and -52, in addition to positions -22, -24, -26, -36, and -38. In vitro methylation reactions demonstrate that the N-terminal extension of HMW FGF-2 acts as a specific substrate for yeast Hmt1p and human HRMT1L2 arginine methyltransferases. These findings indicate that HMW FGF-2, with the presence of five or more dimethylated Gly-Arg-Gly repeats, contains an RGG box-like domain, which may be important for protein-protein and/or protein-RNA interactions.

AB - The post-translational methylation of the N-terminally extended or high molecular weight (HMW) forms of fibroblast growth factor-2 (FGF-2) has been shown to affect the nuclear accumulation of the growth factor. In this study, we determined the extent and position of methyl groups in HMW FGF-2. Using mass spectrometry and amino acid sequence analysis, we have shown that the 22- and 22.5-κDa forms of HMW FGF-2 contain five dimethylated arginines located at positions -22, -24, -26, -36, and -38 using the methionine residue normally used to initiate the 18-κDa form as position 0. The 24-κDa form of HMW FGF-2 contains seven to eight dimethylated arginines located at positions -48, -50, and -52, in addition to positions -22, -24, -26, -36, and -38. In vitro methylation reactions demonstrate that the N-terminal extension of HMW FGF-2 acts as a specific substrate for yeast Hmt1p and human HRMT1L2 arginine methyltransferases. These findings indicate that HMW FGF-2, with the presence of five or more dimethylated Gly-Arg-Gly repeats, contains an RGG box-like domain, which may be important for protein-protein and/or protein-RNA interactions.

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Biochemical analysis of the arginine methylation of high molecular weight fibroblast growth factor-2

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