REVIEW: Cys2His2 Zinc Finger Protein Family: Classification, Functions, and Major Members

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S. V. Razin^1*, V. V. Borunova², O. G. Maksimenko¹, and O. L. Kantidze¹

¹Institute of Gene Biology, Russian Academy of Sciences, ul. Vavilova 34/5, 119334 Moscow, Russia; fax: (499) 135-4105; E-mail: info@genebiology.ru

²Department of Molecular Biology, Biological Faculty, Lomonosov Moscow State University, 119991 Moscow, Russia; fax: (495) 939-4309; E-mail: info@mail.bio.msu.ru

^* To whom correspondence should be addressed.

Received October 3, 2011; Revision received October 19, 2011

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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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KEY WORDS: zinc finger, DNA-binding protein, transcription, regulation of gene expression

DOI: 10.1134/S0006297912030017

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