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Lysine methylation of nonhistone proteins is a way to regulate their stability and function

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Abstract

This review is devoted to the dramatically expanding investigations of lysine methylation on nonhistone proteins and its functional importance. Posttranslational covalent modifications of proteins provide living organisms with ability to rapidly change protein activity and function in response to various stimuli. Enzymatic protein methylation at different lysine residues was evaluated in histones as a part of the “histone code”. Histone methyltransferases methylate not only histones, but also many nuclear and cytoplasmic proteins. Recent data show that the regulatory role of lysine methylation on proteins is not restricted to the “histone code”. This modification modulates activation, stabilization, and degradation of nonhistone proteins, thus influencing numerous cell processes. In this review we particularly focused on methylation of transcription factors and other nuclear nonhistone proteins. The methylated lysine residues serve as markers attracting nuclear “reader” proteins that possess different chromatin-modifying activities.

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Abbreviations

AML1:

acute myeloid leukemia 1 protein

CaM:

calmodulin

ERα:

estrogen receptor α

ESC:

embryonic stem cell

HMT:

histone methyltransferase

PCAF:

p300/CBP-associated factor

PTM:

posttranslational modification

RARα:

retinoic acid receptor α

TAF:

TBP-associated factor

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Authors and Affiliations

  1. Institute of Molecular Genetics, Russian Academy of Sciences, pl. Kurchatova 2, 123182, Moscow, Russia

    K. S. Egorova, O. M. Olenkina & L. V. Olenina

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  2. O. M. Olenkina
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Correspondence to L. V. Olenina.

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Original Russian Text © K. S. Egorova, O. M. Olenkina, L. V. Olenina, 2010, published in Biokhimiya, 2010, Vol. 75, No. 5, pp. 613–628.

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Egorova, K.S., Olenkina, O.M. & Olenina, L.V. Lysine methylation of nonhistone proteins is a way to regulate their stability and function. Biochemistry Moscow 75, 535–548 (2010). https://doi.org/10.1134/S0006297910050019

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