Finger proteins and DNA‐specific recognition: Distinct patterns of conserved amino acids suggest different evolutionary modes

FEBS Letters

Vincent, Alain¹  Payre, François¹ 

[1] Centre de Recherche de Biochimie et Génétique Cellulaires du CNRS, 118, route de Narbonne, 31062 Toulouse Cedex, France

关键词: Finger protein;    DNA binding;    TFIIIA;    Zn2+ chelation;    Transcription activator;    TFIIIA;    transcription factor A of polymerase III;    ICR;    internal control region;    PrKC;    protein kinase C;    C;    cysteine;    F;    phenylalanine;    H;    histidine;    L;    leucine;    Y;    tyrosine;    X;    any amino acid;    GR;    glucocorticoid receptor;    ER;    oestrogen receptor;    PR;    progesterone receptor;    MR;    mineralocorticoid receptor;    UAS;    upstream activation site;   

DOI  :  10.1016/0014-5793(88)80091-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Finger proteins, the first example of which was Xenopus TFIIIA, share Zn²⁺ finger-like folded domains capable of binding to nucleic acids. A large number of this type of protein have been characterised from diverse organisms, indicating a wide evolutionary spread of the DNA-binding fingers. At least two classes of finger proteins may be distinguished. Class I proteins contain variable numbers of the tandemly repeating TFIIIA-like finger motif, (Y/F-X-C-X_2–4-C-X₃-F-X₅-L-X₂-H-X₃-H). Class II finger proteins display a single (C-X₂-C-X₁₃-C-X₂-C) motif and a facultative second putative finger. The relation between the structure of finger proteins and their recognised DNA sequences is discussed.

【 授权许可】

Unknown