Abstract
The protein transcription factor IIIA (TFIII A) is involved in the synthesis of 5S RNA in vitro by RNA polymerase III. It can be isolated from Xenopus laevis oocytes as a 7S particle in which the protein is associated with 5S RNA. Recently it has been shown that the native particle contains 7–11 zinc atoms1. Analysis of the ammo-acid sequence of TFIIIA revealed nine similar domains of approximately 30 amino acids, each containing two invariant pairs of histidines and cysteines, which have been implicated as possible binding sites for the zinc atoms. Other regulatory proteins with sequence homology to the zinc-binding domains of TFIIIA have now been reported2–4. Here, we report the results of an EXAFS (extended X-ray absorption fine structure) study of TFIIIA which shows that the coordination sphere of the zinc sites consists of two cysteine and two histidine residues.
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Diakun, G., Fairall, L. & Klug, A. EXAFS study of the zinc-binding sites in the protein transcription factor IIIA. Nature 324, 698–699 (1986). https://doi.org/10.1038/324698a0
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DOI: https://doi.org/10.1038/324698a0
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