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An altered-specificity mutation in a human POU domain demonstrates functional analogy between the POU-specific subdomain and phage lambda repressor. 总被引:2,自引:0,他引:2
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A Jancso M C Botfield L C Sowers M A Weiss 《Proceedings of the National Academy of Sciences of the United States of America》1994,91(9):3887-3891
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Characterization of chicken octamer-binding proteins demonstrates that POU domain-containing homeobox transcription factors have been highly conserved during vertebrate evolution. 总被引:7,自引:0,他引:7
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B Petryniak L M Staudt C E Postema W T McCormack C B Thompson 《Proceedings of the National Academy of Sciences of the United States of America》1990,87(3):1099-1103
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The embryonic stem cell transcription factors Oct-4 and FoxD3 interact to regulate endodermal-specific promoter expression 总被引:17,自引:0,他引:17
Guo Y Costa R Ramsey H Starnes T Vance G Robertson K Kelley M Reinbold R Scholer H Hromas R 《Proceedings of the National Academy of Sciences of the United States of America》2002,99(6):3663-3667
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Differential expression of four members of the POU family of proteins in activated and phorbol 12-myristate 13-acetate-treated Jurkat T cells. 总被引:4,自引:1,他引:3
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A K Bhargava Z Li S M Weissman 《Proceedings of the National Academy of Sciences of the United States of America》1993,90(21):10260-10264
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Ilaria Baglivo Luigi Russo Sabrina Esposito Gaetano Malgieri Mario Renda Antonio Salluzzo Benedetto Di Blasio Carla Isernia Roberto Fattorusso Paolo V. Pedone 《Proceedings of the National Academy of Sciences of the United States of America》2009,106(17):6933-6938
The recent characterization of the prokaryotic Cys2His2 zinc-finger domain, identified in Ros protein from Agrobacterium tumefaciens, has demonstrated that, although possessing a similar zinc coordination sphere, this domain is structurally very different from its eukaryotic counterpart. A search in the databases has identified ≈300 homologues with a high sequence identity to the Ros protein, including the amino acids that form the extensive hydrophobic core in Ros. Surprisingly, the Cys2His2 zinc coordination sphere is generally poorly conserved in the Ros homologues, raising the question of whether the zinc ion is always preserved in these proteins. Here, we present a functional and structural study of a point mutant of Ros protein, Ros56–142C82D, in which the second coordinating cysteine is replaced by an aspartate, 5 previously-uncharacterized representative Ros homologues from Mesorhizobium loti, and 2 mutants of the homologues. Our results indicate that the prokaryotic zinc-finger domain, which in Ros protein tetrahedrally coordinates Zn(II) through the typical Cys2His2 coordination, in Ros homologues can either exploit a CysAspHis2 coordination sphere, previously never described in DNA binding zinc finger domains to our knowledge, or lose the metal, while still preserving the DNA-binding activity. We demonstrate that this class of prokaryotic zinc-finger domains is structurally very adaptable, and surprisingly single mutations can transform a zinc-binding domain into a nonzinc-binding domain and vice versa, without affecting the DNA-binding ability. In light of our findings an evolutionary link between the prokaryotic and eukaryotic zinc-finger domains, based on bacteria-to-eukaryota horizontal gene transfer, is discussed. 相似文献
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Mark Hilge Jan Aelen Alice Foarce Anastassis Perrakis Geerten W. Vuister 《Proceedings of the National Academy of Sciences of the United States of America》2009,106(34):14333-14338
Regulation of ion-transport in the Na+/Ca2+ exchanger (NCX) occurs via its cytoplasmic Ca2+-binding domains, CBD1 and CBD2. Here, we present a mechanism for NCX activation and inactivation based on data obtained using NMR, isothermal titration calorimetry (ITC) and small-angle X-ray scattering (SAXS). We initially determined the structure of the Ca2+-free form of CBD2-AD and the structure of CBD2-BD that represent the two major splice variant classes in NCX1. Although the apo-form of CBD2-AD displays partially disordered Ca2+-binding sites, those of CBD2-BD are entirely unstructured even in an excess of Ca2+. Striking differences in the electrostatic potential between the Ca2+-bound and -free forms strongly suggest that Ca2+-binding sites in CBD1 and CBD2 form electrostatic switches analogous to C2-domains. SAXS analysis of a construct containing CBD1 and CBD2 reveals a conformational change mediated by Ca2+-binding to CBD1. We propose that the electrostatic switch in CBD1 and the associated conformational change are necessary for exchanger activation. The response of the CBD1 switch to intracellular Ca2+ is influenced by the closely located cassette exons. We further propose that Ca2+-binding to CBD2 induces a second electrostatic switch, required to alleviate Na+-dependent inactivation of Na+/Ca2+ exchange. In contrast to CBD1, the electrostatic switch in CBD2 is isoform- and splice variant-specific and allows for tailored exchange activities. 相似文献
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Combined pituitary hormone deficiency caused by compound heterozygosity for two novel mutations in the POU domain of the Pit1/POU1F1 gene 总被引:1,自引:0,他引:1
Hendriks-Stegeman BI Augustijn KD Bakker B Holthuizen P van der Vliet PC Jansen M 《The Journal of clinical endocrinology and metabolism》2001,86(4):1545-1550