scholarly journals Loss-of-function mutations in Zn-finger DNA-binding domain of HNF4A cause aberrant transcriptional regulation in liver cancer

Oncotarget ◽  
2018 ◽  
Vol 9 (40) ◽  
pp. 26144-26156 ◽  
Author(s):  
Hiroaki Taniguchi ◽  
Akihiro Fujimoto ◽  
Hidetoshi Kono ◽  
Mayuko Furuta ◽  
Masashi Fujita ◽  
...  
Keyword(s):  
Transcriptional Regulation ◽  
Dna Binding ◽  
Liver Cancer ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Loss Of Function

scholarly journals An unexpected role for Dicer as a reader of the unacetylated DNA binding domain of p53 in transcriptional regulation

2021 ◽  
Vol 7 (44) ◽  
Author(s):  
Xin Yang ◽  
Xingwu Wang ◽  
Zhiming Li ◽  
Shoufu Duan ◽  
Huan Li ◽  
...  
Keyword(s):  
Transcriptional Regulation ◽  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain

scholarly journals Presence and significance of a R110W mutation in the DNA-binding domain of GCM2 gene in patients with isolated hypoparathyroidism and their family members

2010 ◽  
Vol 162 (2) ◽  
pp. 407-421 ◽  
Author(s):  
Neeraj Tomar ◽  
Hema Bora ◽  
Ratnakar Singh ◽  
Nandita Gupta ◽  
Punit Kaur ◽  
...  
Keyword(s):  
Dna Binding ◽  
Nuclear Localization ◽  
Family Members ◽  
Binding Domain ◽  
Compound Heterozygous ◽  
Dna Binding Domain ◽  
Nucleotide Polymorphisms ◽  
Loss Of Function ◽  
Mobility Shift ◽  
Mobility Shift Assay

ObjectiveGlial cells missing 2 (GCM2) gene encodes a parathyroid-specific transcription factor. We assessed GCM2 gene sequence in patients with isolated hypoparathyroidism (IH).DesignCase–control study.MethodsComplete DNA sequencing of the GCM2 gene including its exons, promoter, and 5′ and 3′ UTRs was performed in 24/101 patients with IH. PCR–restriction fragment length polymorphism was used to detect a novel R110W mutation in all 101 IH patients and 655 healthy controls. Significance of the mutation was assessed by electrophoretic mobility shift assay (EMSA) and nuclear localization on transfection.ResultsA heterozygous R110W mutation was present in DNA-binding domain in 11/101 patients (10.9%) and absent in 655 controls (P<10−7). Four of 13 nonaffected first-degree relatives for five of these index cases had R110W mutation. Four heterozygous single nucleotide polymorphisms were found in the 5′ region. One of the 11 patients with R110W also had T370M change in compound heterozygous form. Mutant R110W and T370M GCM2 proteins showed decreased binding with GCM recognition elements on EMSA indicating loss of function. Both wild-type and R110W mutant GCM2 proteins showed nuclear localization.ConclusionsThe present study indicates a significant association of R110W variant with IH. Absence of effect of heterozygous R110W mutation on DNA binding and presence of the same mutation in asymptomatic family members indicate that additional genetic (akin to T370M change) or nongenetic factors might contribute to the expression of diseases in IH. Alternatively, it is possible that association of R110W with IH could be due to linkage disequilibrium with the unidentified relevant genes in IH.

NMR studies of the R2 repeat and related peptide fragments of the DNA binding domain of c-Myb. New light on the structure and folding of R2.

1999 ◽  
Vol 96 (9/10) ◽  
pp. 1580-1584 ◽  
Author(s):  
I. Ségalas ◽  
S. Desjardins ◽  
H. Oulyadi ◽  
Y. Prigent ◽  
S. Tribouillard ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Peptide Fragments ◽  
Nmr Studies ◽  
Related Peptide

scholarly journals Primary structure of a glycosylated DNA-binding domain in human plasma fibronectin.

1985 ◽  
Vol 260 (4) ◽  
pp. 2301-2306
Author(s):  
H Pande ◽  
J Calaycay ◽  
D Hawke ◽  
C M Ben-Avram ◽  
J E Shively
Keyword(s):  
Dna Binding ◽  
Human Plasma ◽  
Primary Structure ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Plasma Fibronectin
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