Zinc(II) ions selectively interact with DNA sequences present at the TFIIIA binding site of the Xenopus 5S-RNA gene
- PMID: 7630723
- PMCID: PMC307052
- DOI: 10.1093/nar/23.13.2464
Zinc(II) ions selectively interact with DNA sequences present at the TFIIIA binding site of the Xenopus 5S-RNA gene
Abstract
It has been known for some time that zinc, as well as most transition metal ions, is capable of binding to the DNA bases. However, little is known about the presence and distribution of metal binding sites along naturally occurring genomic DNA molecules. In this paper, the interaction of zinc with the Xenopus 5S-RNA gene has been studied and several metal binding sites have been identified on the basis of the changes in chemical reactivity observed in the presence of the metal. The strongest zinc-binding sites of the Xenopus 5S-RNA gene correspond to GGG trinucleotide repeats. Some GG dinucleotides also show a significant affinity for zinc. Interestingly, the binding site for TFIIIA, a zinc-finger transcription factor, contains several sites with strong zinc affinity. In particular, a TGGGA sequence which is essential for the binding of TFIIIA shows the strongest affinity for zinc. The conformational properties of this DNA sequence, together with the high electronegative potential of GGG runs, is likely to determine its strong affinity for zinc. The possible biological relevance of these results is discussed.
Similar articles
-
Contribution of individual amino acids to the nucleic acid binding activities of the Xenopus zinc finger proteins TFIIIIA and p43.Biochemistry. 2001 May 22;40(20):6093-101. doi: 10.1021/bi0025215. Biochemistry. 2001. PMID: 11352746
-
Effects of zinc finger mutations on the nucleic acid binding activities of Xenopus transcription factor IIIA.Biochemistry. 1995 Nov 28;34(47):15545-52. doi: 10.1021/bi00047a021. Biochemistry. 1995. PMID: 7492557
-
Specific interaction of the first three zinc fingers of TFIIIA with the internal control region of the Xenopus 5 S RNA gene.J Mol Biol. 1992 Feb 20;223(4):857-71. doi: 10.1016/0022-2836(92)90248-i. J Mol Biol. 1992. PMID: 1538401
-
Transcription factor IIIA (TFIIIA): an update.Experientia. 1993 Oct 15;49(10):831-5. doi: 10.1007/BF01952592. Experientia. 1993. PMID: 8224095 Review.
-
Metal requirements for nucleic acid binding proteins.Methods Enzymol. 1991;208:46-54. doi: 10.1016/0076-6879(91)08006-4. Methods Enzymol. 1991. PMID: 1779843 Review. No abstract available.
Cited by
-
Preferential binding and structural distortion by Fe2+ at RGGG-containing DNA sequences correlates with enhanced oxidative cleavage at such sequences.Nucleic Acids Res. 2005 Jan 19;33(2):497-510. doi: 10.1093/nar/gki192. Print 2005. Nucleic Acids Res. 2005. PMID: 15659581 Free PMC article.
-
Unusually wide co-factor tolerance in a metalloenzyme; divalent metal ions modulate endo-exonuclease activity in T5 exonuclease.Nucleic Acids Res. 2001 Jul 1;29(13):2772-9. doi: 10.1093/nar/29.13.2772. Nucleic Acids Res. 2001. PMID: 11433022 Free PMC article.
-
In silico structural analysis of sequences containing 5-hydroxymethylcytosine reveals its potential as binding regulator for development, ageing and cancer-related transcription factors.Epigenetics. 2021 May;16(5):503-518. doi: 10.1080/15592294.2020.1805693. Epub 2020 Sep 2. Epigenetics. 2021. PMID: 32752914 Free PMC article.
-
The Bacillus subtilis regulator SinR inhibits spoIIG promoter transcription in vitro without displacing RNA polymerase.Nucleic Acids Res. 1998 Aug 15;26(16):3806-12. doi: 10.1093/nar/26.16.3806. Nucleic Acids Res. 1998. PMID: 9685500 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources