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Related Experiment Video

Updated: May 26, 2026

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy

Published on: December 16, 2021

Modulating protein activity and cellular function by methionine residue oxidation.

Zong Jie Cui¹, Zong Qiang Han, Zhi Ying Li

¹Institute of Cell Biology, Beijing Normal University, Beijing 100875, China. zjcui@bnu.edu.cn

|December 8, 2011

Summary

This summary is machine-generated.

Methionine oxidation to methionine sulfoxide in proteins is common and impacts cellular functions. This controlled oxidation can be a tool to study protein activity.

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Area of Science:

Biochemistry
Molecular Biology
Cellular Biology

Background:

Methionine (Met), a sulfur-containing amino acid, is susceptible to oxidation into methionine sulfoxide [Met(O)] by reactive oxygen species.
This oxidation occurs in vitro and in vivo, affecting numerous critical proteins.

Purpose of the Study:

To summarize the diverse roles of methionine oxidation in protein function and cellular activity.
To highlight the potential of controlled methionine oxidation as an 'oxigenetics' tool.

Main Methods:

Literature review of studies on methionine oxidation in various proteins.
Analysis of the functional consequences of Met sulfoxidation on protein activity and cellular processes.

Main Results:

Methionine sulfoxidation activates key signaling proteins like calcium/calmodulin-dependent protein kinase II and ion channels.
It also inhibits the fibrillation of proteins implicated in atherosclerosis and neurodegenerative diseases (e.g., amyloid beta, α-synuclein).
Methionine oxidation correlates with significant alterations in cellular activities.

Conclusions:

Methionine oxidation is a widespread post-translational modification with profound effects on protein function.
Controlled Met oxidation offers a novel approach for dissecting specific protein functions in situ.