Structural Analyses of Zinc Finger Domains for Specific Interactions with DNA

• Published in: Journal of microbiology and biotechnology Vol. 26; no. 12; pp. 2019 - 2029
• Main Authors: Eom, Ki Seong, Cheong, Jin Sung, Lee, Seung Jae
• Format: Journal Article
• Language: English
• Published: Korea (South) 한국미생물·생명공학회 28.12.2016
• Subjects: Bacteria - chemistry; Bacteria - genetics; Bacteria - metabolism; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; DNA, Bacterial - chemistry; DNA, Bacterial - genetics; DNA, Bacterial - metabolism; Protein Binding; Zinc Fingers; 생물학; classical zinc finger; Zinc finger proteins; transcriptional regulator; metalloproteins
• ISSN: 1017-7825; 1738-8872
• DOI: 10.4014/jmb.1609.09021

Zinc finger proteins are among the most extensively applied metalloproteins in the field of biotechnology owing to their unique structural and functional aspects as transcriptional and translational regulators. The classical zinc fingers are the largest family of zinc proteins and they provide critical roles in physiological systems from prokaryotes to eukaryotes. Two cysteine and two histidine residues (Cys₂His₂) coordinate to the zinc ion for the structural functions to generate a ββα fold, and this secondary structure supports specific interactions with their binding partners, including DNA, RNA, lipids, proteins, and small molecules. In this account, the structural similarity and differences of well-known Cys₂His₂-type zinc fingers such as zinc interaction factor 268 (ZIF268), transcription factor IIIA (TFIIIA), GAGA, and Ros will be explained. These proteins perform their specific roles in species from archaea to eukaryotes and they show significant structural similarity; however, their aligned amino acids present low sequence homology. These zinc finger proteins have different numbers of domains for their structural roles to maintain biological progress through transcriptional regulations from exogenous stresses. The superimposed structures of these finger domains provide interesting details when these fingers are applied to specific gene binding and editing. The structural information in this study will aid in the selection of unique types of zinc finger applications in vivo and in vitro approaches, because biophysical backgrounds including complex structures and binding affinities aid in the protein design area.