Payre F, Vincent A
Centre de Recherche de Biochimie et Génétique Cellulaires du CNRS, Toulouse, France.
FEBS Lett. 1988 Jul 18;234(2):245-50. doi: 10.1016/0014-5793(88)80091-7.
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-X2-4-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.
手指蛋白的首个例子是非洲爪蟾的TFIIIA，它具有能够与核酸结合的锌指样折叠结构域。已从多种生物体中鉴定出大量此类蛋白质，这表明DNA结合指在进化上分布广泛。至少可以区分出两类手指蛋白。I类蛋白含有数量可变的串联重复TFIIIA样指基序（Y/F-X-C-X2-4-C-X3-F-X5-L-X2-H-X3-H）。II类手指蛋白呈现单个（C-X2-C-X13-C-X2-C）基序和一个兼性的第二个推定指。本文讨论了手指蛋白的结构与其识别的DNA序列之间的关系。
