Zinc transfer from transcription factor IIIA fingers to thionein clusters.
نویسندگان
چکیده
منابع مشابه
Importance of minor groove binding zinc fingers within the transcription factor IIIA-DNA complex.
The gene-specific transcription factor IIIA (TFIIIA) binds to the internal promoter element of the 5 S rRNA gene through nine zinc fingers which make specific DNA contacts. Seven of the nine TFIIIA zinc fingers participate in major groove DNA contacts while two fingers, 4 and 6, have been proposed to bind in or across the minor groove. Pyrrole-imidazole polyamides are minor groove binding ligan...
متن کاملControl of zinc transfer between thionein, metallothionein, and zinc proteins.
Metallothionein (MT), despite its high metal binding constant (KZn = 3.2 x 10(13) M-1 at pH 7.4), can transfer zinc to the apoforms of zinc enzymes that have inherently lower stability constants. To gain insight into this paradox, we have studied zinc transfer between zinc enzymes and MT. Zinc can be transferred in both directions-i.e., from the enzymes to thionein (the apoform of MT) and from ...
متن کاملAssessment of major and minor groove DNA interactions by the zinc fingers of Xenopus transcription factor IIIA
Zinc finger proteins of the Cys2His2 class are DNA sequence-specific transcription factors. Previous structural studies of zinc finger protein-DNA complexes have shown that amino acids in the finger tip and alpha-helix regions within individual finger domains make base-specific contacts with the major groove of DNA. The nine finger protein transcription factor IIIA (TFIIIA) from Xenopus oocytes...
متن کاملDiffering roles for zinc fingers in DNA recognition: structure of a six-finger transcription factor IIIA complex.
The crystal structure of the six NH2-terminal zinc fingers of Xenopus laevis transcription factor IIIA (TFIIIA) bound with 31 bp of the 5S rRNA gene promoter has been determined at 3.1 A resolution. Individual zinc fingers are positioned differently in the major groove and across the minor groove of DNA to span the entire length of the duplex. These results show how TFIIIA can recognize several...
متن کاملMetal-dependent folding of a single zinc finger from transcription factor IIIA.
A 30-amino acid peptide, which corresponds to the second "zinc finger" domain of transcription factor IIIA, has been synthesized and purified. This peptide folds in the presence of zinc: adding Zn2+ significantly changes the circular dichroism spectrum, and Zn2+ protects the peptide from tryptic digestion. The peptide also binds Co2+, and the absorption spectrum of the Co2+ complex suggests tha...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1991
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.88.22.9984