Journal
BIOCHEMISTRY
Volume 43, Issue 26, Pages 8346-8355Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi035673j
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Funding
- NIGMS NIH HHS [1 R01 GM58183-01A1] Funding Source: Medline
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Vertebrate GATA proteins regulate processes that are vital to development, and each possesses two tandem GATA finger domains: an N-terminal GATA finger and a C-terminal GATA finger. These GATA fingers require Zn2+ to fold, to bind DNA recognition elements, and to regulate transcription. While the GATA-I C-terminal finger is necessary and sufficient to bind to single GATA DNA sites, the N-terminal finger interacts with DNA such that the double finger unit (DF domain) has a binding and transactivation profile that is tuned by the DNA-binding site. Co2+ was used as a spectroscopic probe in a series of competition titrations to determine the affinity of Co2+ and Zn2+ for the C-terminal finger from chicken GATA-I and the double finger from human GATA-1 (referred to in this report as CF and DF). For CF, these experiments yielded K-b(Co) = 1.0 (+/-1.3) x 10(7) M-1 and K-b(Zn) = 2.0 (+/-1.3) x 10(10) M-1. For DF, these experiments yielded equilibrium constants for the process of two M2+ binding to form M-2(2+)-DF of beta(2)(Co) = 2.5 (+/-1.6) x 10(14) M-2 and beta(2)(Zn) = 6.3 (+/-2.5) x 10(20) M-2. The ZnS4 coordination environment of Zn2+-bound CF was confirmed with X-ray absorption spectroscopy. A detailed analysis of these data suggests that the N-terminal and C-terminal fingers of DF act as independent and identical Zn2+-binding sites and each finger binds Zn2+ with an affinity equivalent to that of CF.
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