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Related Experiment Video

Updated: Jun 19, 2026

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

Published on: August 7, 2021

Heterogeneous nuclear RNP protein A1-arginine methylation during HCT-48 cell cycle.

S H Park¹, G H Park, H Gu

¹Department of Biochemistry, Korea University Medical School, Seoul, Korea,Graduate School of Biotechnology, Korea University Medical School, Seoul, Korea.

Biochemistry and Molecular Biology International

|October 27, 2009

Summary

Protein methylase I activity increases during the cell cycle, peaking in S phase. This enzyme methylates hnRNP protein A1 and endogenous 20-kDa proteins, suggesting a role in post-translational modification.

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Studying Cell Cycle-regulated Gene Expression by Two Complementary Cell Synchronization Protocols

Studying Cell Cycle-regulated Gene Expression by Two Complementary Cell Synchronization Protocols

Published on: June 6, 2017

Area of Science:

Cellular biology
Molecular biology
Biochemistry

Background:

Protein methylase I, also known as protein-arginine N-methyltransferase, catalyzes the methylation of arginine residues in proteins.
Post-translational modifications like methylation play crucial roles in regulating protein function and cellular processes.

Purpose of the Study:

To investigate the activity and substrate specificity of Protein methylase I during the cell cycle in HCT-48 cells.
To identify the specific methylation products and endogenous substrates of Protein methylase I.

Main Methods:

Cell synchronization using serum deprivation and hydroxyurea treatment.
Enzyme activity assays using exogenously added hnRNP protein A1.
SDS-PAGE/fluorography and HPLC for identification of methylated products and substrates.

Main Results:

Protein methylase I activity showed a 2-fold increase from G0 to S phase, followed by a decrease in G2/M phase.
HPLC analysis identified NG-monomethylarginine and NG,NG-dimethylarginines as methylation products.
A 20-kDa endogenous protein was intensely methylated, and its methylation was inhibited by exogenous hnRNP protein A1, indicating substrate competition.

Conclusions:

Protein methylase I activity is cell cycle-dependent, with peak activity during the S phase.
hnRNP protein A1 and a 20-kDa endogenous protein are substrates for Protein methylase I, suggesting a role in regulating protein function through methylation.