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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제26권 제12호
- 발행연도
- 2016.12
- 수록면
- 2,019 - 2,029 (11page)
- DOI
- 10.4014/jmb.1609.09021
이용수
초록· 키워드
오류제보하기
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.
목차
등록된 정보가 없습니다.
참고문헌 (78)
참고문헌 신청
Archdeacon J / 2000 / A single amino acid substitution beyond the C2H2-zinc finger in Ros derepresses virulence and T-DNA genes in Agrobacterium tumefaciens / FEMS Microbiol. Lett 187:175~178
Bai CY / 1998 / Drosophila clipper/CPSF 30K is a post-transcriptionally regulated nuclear protein that binds RNA containing GC clusters / Nucleic Acids Res 26:1597~1604
Beckmann AM / 1997 / Differential expression of Egr-1-like DNA-binding activities in the naive rat brain and after excitatory stimulation / J. Neurochem 69:2227~2237
Beckmann AM / 1997 / Egr transcription factors in the nervous system / Neurochem. Int 31:477~510
Beerli RR / 2002 / Engineering polydactyl zincfinger transcription factors / Nat. Biotechnol 20:135~141
Bai CY / 1998 / Drosophila clipper/CPSF 30K is a post-transcriptionally regulated nuclear protein that binds RNA containing GC clusters / Nucleic Acids Res 26:1597~1604
Beckmann AM / 1997 / Differential expression of Egr-1-like DNA-binding activities in the naive rat brain and after excitatory stimulation / J. Neurochem 69:2227~2237
Beckmann AM / 1997 / Egr transcription factors in the nervous system / Neurochem. Int 31:477~510
Beerli RR / 2002 / Engineering polydactyl zincfinger transcription factors / Nat. Biotechnol 20:135~141
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