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Cys2His2 zinc finger protein family: Classification, functions, and major members

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Abstract

Cys2His2 (C2H2)-type zinc fingers are widespread DNA binding motifs in eukaryotic transcription factors. Zinc fingers are short protein motifs composed of two or three β-layers and one α-helix. Two cysteine and two histidine residues located in certain positions bind zinc to stabilize the structure. Four other amino acid residues localized in specific positions in the N-terminal region of the α-helix participate in DNA binding by interacting with hydrogen donors and acceptors exposed in the DNA major groove. The number of zinc fingers in a single protein can vary over a wide range, thus enabling variability of target DNA sequences. Besides DNA binding, zinc fingers can also provide protein-protein and RNA-protein interactions. For the most part, proteins containing the C2H2-type zinc fingers are trans regulators of gene expression that play an important role in cellular processes such as development, differentiation, and suppression of malignant cell transformation (oncosuppression).

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Abbreviations

a.a.:

amino acid residue

C2H2:

Cys2His2

ZF:

zinc finger

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Authors and Affiliations

  1. Institute of Gene Biology, Russian Academy of Sciences, ul. Vavilova 34/5, 119334, Moscow, Russia

    S. V. Razin, O. G. Maksimenko & O. L. Kantidze

  2. Department of Molecular Biology, Biological Faculty, Lomonosov Moscow State University, 119991, Moscow, Russia

    V. V. Borunova

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  1. S. V. Razin
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Original Russian Text © S. V. Razin, V. V. Borunova, O. G. Maksimenko, O. L. Kantidze, 2012, published in Biokhimiya, 2012, Vol. 77, No. 3, pp. 277–288.

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Razin, S.V., Borunova, V.V., Maksimenko, O.G. et al. Cys2His2 zinc finger protein family: Classification, functions, and major members. Biochemistry Moscow 77, 217–226 (2012). https://doi.org/10.1134/S0006297912030017

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