Zinc Fingers: A Novel Protein Fold for Nucleic Acid Recognition

  1. A. Klug and
  2. D. Rhodes
  1. MRC Laboratory of Molecular Biology, Cambridge CB2 2QH, England

This extract was created in the absence of an abstract.

Excerpt

An essential part of gene expression and regulation is the binding of a regulatory protein to the recognition sequence of the gene on which it acts. Many such proteins have embedded in their structures a domain, or motif, that serves for binding to DNA. The best-understood protein structure used for DNA binding is the helix-turn-helix motif seen in the crystal structure of several bacterial regulatory proteins (for review, see Pabo and Sauer 1984; Anderson et al. 1987). Amino acid sequences that could form a similar structural motif are also present in the homeo box region of several eukaryotic proteins (Gehring 1985).

A few years ago, it was discovered in this laboratory (Miller et al. 1985) that the Xenopus transcription factor IIIA (TFIIIA) for the 5S RNA gene contains small sequence units repeated in tandem, and it was proposed that each unit is folded about a Zn atom to form separate...

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