scholarly journals Gamma Radiation-Induced Damage in the Zinc Finger of the Transcription Factor IIIA

2016 ◽  
Vol 2016 ◽  
pp. 1-7 ◽  
Author(s):  
XiaoHong Zhang ◽  
YuJi Miao ◽  
XiaoDan Hu ◽  
Rui Min ◽  
PeiDang Liu ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Ionizing Radiation ◽  
Gamma Radiation ◽  
Zinc Finger ◽  
Cysteine Residues ◽  
Zinc Finger Motif ◽  
Thiol Groups ◽  
Transcription Factor Iiia ◽  
Zinc Finger Motifs ◽  
Radiation Induced

A zinc finger motif is an element of proteins that can specifically recognize and bind to DNA. Because they contain multiple cysteine residues, zinc finger motifs possess redox properties. Ionizing radiation generates a variety of free radicals in organisms. Zinc finger motifs, therefore, may be a target of ionizing radiation. The effect of gamma radiation on the zinc finger motifs in transcription factor IIIA (TFIIIA), a zinc finger protein, was investigated. TFIIIA was exposed to different gamma doses from 60Co sources. The dose rates were 0.20 Gy/min and 800 Gy/h, respectively. The binding capacity of zinc finger motifs in TFIIIA was determined using an electrophoretic mobility shift assay. We found that 1000 Gy of gamma radiation impaired the function of the zinc finger motifs in TFIIIA. The sites of radiation-induced damage in the zinc finger were the thiol groups of cysteine residues and zinc (II) ions. The thiol groups were oxidized to form disulfide bonds and the zinc (II) ions were indicated to be reduced to zinc atoms. These results indicate that the zinc finger motif is a target domain for gamma radiation, which may decrease 5S rRNA expression via impairment of the zinc finger motifs in TFIIIA.

scholarly journals A novel ionizing radiation-induced signaling pathway that activates the transcription factor NF-κB

Oncogene ◽  
1998 ◽  
Vol 17 (14) ◽  
pp. 1821-1826 ◽  
Author(s):  
Su-Jae Lee ◽  
Alexandre Dimtchev ◽  
Martin F Lavin ◽  
Anatoly Dritschilo ◽  
Mira Jung
Keyword(s):  
Transcription Factor ◽  
Ionizing Radiation ◽  
Signaling Pathway ◽  
Radiation Induced

scholarly journals Sequence of the HAP3 transcription factor of Kluyveromyces lactis predicts the presence of a novel 4-cysteine zinc-finger motif

1994 ◽  
Vol 245 (1) ◽  
pp. 96-106 ◽  
Author(s):  
Wietse Mulder ◽  
Inge H. J. M. Scholten ◽  
René W. de Boer ◽  
Leslie A. Grivell
Keyword(s):  
Transcription Factor ◽  
Zinc Finger ◽  
Kluyveromyces Lactis ◽  
Zinc Finger Motif

scholarly journals Functional analyses of the CIF1-CIF2 complex in Trypanosoma brucei identify the structural motifs required for complex formation and cytokinesis

2017 ◽  
Author(s):  
Huiqing Hu ◽  
Paul Majneri ◽  
Dielan Li ◽  
Yasuhiro Kurasawa ◽  
Tai An ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Coiled Coil ◽  
Longitudinal Axis ◽  
Zinc Finger Motif ◽  
Structural Motifs ◽  
Zinc Finger Motifs ◽  
Ef Hand ◽  
Functional Analyses ◽  
Attachment Zone ◽  
Structural Insights

ABSTRACTCytokinesis in trypanosome occurs uni-directionally along the longitudinal axis from the cell anterior towards the cell posterior and requires a trypanosome-specific CIF1-CIF2 protein complex. However, little is known about the contribution of the structural motifs in CIF1 and CIF2 to complex assembly and cytokinesis. Here, we demonstrated that the two zinc-finger motifs but not the coiled-coil motif in CIF1 are required for interaction with the EF-hand motifs in CIF2. We further showed that localization of CIF1 depends on the coiled-coil motif and the first zinc-finger motif and that localization of CIF2 depends on the EF-hand motifs. Deletion of the coiled-coil motif and mutation of either zinc-finger motifs in CIF1 disrupted cytokinesis. Further, mutation of either zinc-finger motif in CIF1 mis-localized CIF2 to the cytosol and destabilized CIF2, whereas deletion of the coiled-coil motif in CIF1 spread CIF2 over to the new flagellum attachment zone and stabilized CIF2. Together, these results uncovered the requirement of the coiled-coil motif and zinc-finger motifs for CIF1 function in cytokinesis and for CIF2 localization and stability, providing structural insights into the functional interplay between the two cytokinesis regulators.

klumpfuss, a Drosophila gene encoding a member of the EGR family of transcription factors, is involved in bristle and leg development

Development ◽  
1997 ◽  
Vol 124 (16) ◽  
pp. 3123-3134 ◽  
Author(s):  
T. Klein ◽  
J.A. Campos-Ortega
Keyword(s):  
Transcription Factor ◽  
Zinc Finger ◽  
Wilms Tumor ◽  
Suppressor Gene ◽  
Transcription Unit ◽  
Gene Encoding ◽  
Zinc Finger Motifs ◽  
Leg Development ◽  
Putative Transcription Factor ◽  
Mother Cells

The klumpfuss (klu) transcription unit in Drosophila gives rise to two different transcripts of 4.5 and 4.9 kb, both of which encode a putative transcription factor with four zinc-finger motifs of the C2H2 class. Zinc-finger 2–4 are homologous to those of the proteins of the EGR transcription factor family. As in the case of the most divergent member of the family, the Wilms' tumor suppressor gene (WT-1), klu contains an additional zinc finger, which is only distantly related. Loss of klumpfuss function is semilethal and causes a variety of defects in bristles and legs of adults, as well as in mouth hooks and brains of larvae. Analysis of the mutants indicates that klumpfuss is required for proper specification and differentiation of a variety of cells, including the sensory organ mother cells and those of the distal parts of tarsal segments.

THE TEMPORAL RESPONSE OF RECOMBINATION EVENTS TO GAMMA RADIATION OF MEIOTIC CELLS IN SORDARIA BREVICOLLIS

1982 ◽  
Vol 24 (5) ◽  
pp. 505-519 ◽  
Author(s):  
Leslie A. Lewis
Keyword(s):  
Ionizing Radiation ◽  
Gamma Radiation ◽  
Recombination Frequency ◽  
S Phase ◽  
Temporal Response ◽  
Prophase I ◽  
Radiation Induced ◽  
Meiotic Cycle

The temporal frequencies of different stages of prophase I were determined cytologically in Sordaria brevicollis (Olive and Fantini) as the basis for ascertaining the degree of synchrony in meiosis in this ascomycete. Croziers, karyogamy-zygotene and pachytene asci were shown to be in significant majorities at three distinct periods of the meiotic cycle. The response of recombination frequency to ionizing radiation was examined for the entire meiotic cycle. Three radiosensitive periods were determined. This response, which correlated temporally with each of the three peaks in ascal frequency, is interpreted as showing that the meiotic cycle of this organism is divided into periods of recombination commitment (radiation reduced frequencies) during the pre-meiotic S phase and recombination consummation (radiation induced frequencies) during zygotene and pachytene. The results are discussed in the context of the time at which recombination is consummated in eukaryotes such as yeast and Drosophila.

scholarly journals Inhibition of red blood cell development by arsenic-induced disruption of GATA-1

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Xixi Zhou ◽  
Sebastian Medina ◽  
Alicia M. Bolt ◽  
Haikun Zhang ◽  
Guanghua Wan ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Zinc Finger ◽  
Zinc Fingers ◽  
Arsenic Exposure ◽  
In Vivo Studies ◽  
Regulatory Factor ◽  
Zinc Finger Motifs ◽  
First Time

Abstract Anemia is a hematological disorder that adversely affects the health of millions of people worldwide. Although many variables influence the development and exacerbation of anemia, one major contributing factor is the impairment of erythropoiesis. Normal erythropoiesis is highly regulated by the zinc finger transcription factor GATA-1. Disruption of the zinc finger motifs in GATA-1, such as produced by germline mutations, compromises the function of this critical transcription factor and causes dyserythropoietic anemia. Herein, we utilize a combination of in vitro and in vivo studies to provide evidence that arsenic, a widespread environmental toxicant, inhibits erythropoiesis likely through replacing zinc within the zinc fingers of the critical transcription factor GATA-1. We found that arsenic interacts with the N- and C-terminal zinc finger motifs of GATA-1, causing zinc loss and inhibition of DNA and protein binding activities, leading to dyserythropoiesis and an imbalance of hematopoietic differentiation. For the first time, we show that exposures to a prevalent environmental contaminant compromises the function of a key regulatory factor in erythropoiesis, producing effects functionally similar to inherited GATA-1 mutations. These findings highlight a novel molecular mechanism by which arsenic exposure may cause anemia and provide critical insights into potential prevention and intervention for arsenic-related anemias.

scholarly journals Identification of DNA Recognition Sequences and Protein Interaction Domains of the Multiple-Zn-Finger Protein Roaz

1998 ◽  
Vol 18 (11) ◽  
pp. 6447-6456 ◽  
Author(s):  
Robert Y. L. Tsai ◽  
Randall R. Reed
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Binding Site ◽  
Zinc Finger ◽  
Protein Interaction ◽  
Inverted Repeat ◽  
Finger Protein ◽  
Zinc Finger Motifs ◽  
Half Site

ABSTRACT Roaz, a rat C2H2 zinc finger protein, plays a role in the regulation of olfactory neuronal differentiation through its interaction with the Olf-1/EBF transcription factor family. An additional role for the Roaz/Olf-1/EBF heterodimeric protein is suggested by its ability to regulate gene activation at a distinct promoter lacking Olf-1/EBF-binding sites. Using an in vitro binding-site selection assay (Selex), we demonstrate that Roaz protein binds to novel inverted perfect or imperfect repeats of GCACCC separated by 2 bp. We show that Roaz is capable of binding to a canonical consensus recognition sequence with high affinity (Kd = 3 nM). Analysis of the structural requirement for protein dimerization and DNA binding by Roaz reveals the role of specific zinc finger motifs in the Roaz protein for homodimerization and heterodimerization with the Olf-1/EBF transcription factor. The DNA-binding domain of Roaz is mapped to the N-terminal 277 amino acids, containing the first seven zinc finger motifs, which confers weak monomeric binding to a single half site and a stronger dimeric binding to the inverted repeat in a binding-site-dependent manner. Full-length protein can form dimers on both the inverted repeat and direct repeat but not on a single half site. These findings support the role of the TFIIIA-type Zn fingers in both protein-protein interaction and protein-DNA interaction and suggest distinct functions for specific motifs in proteins with a large number of zinc finger structures.

Sign in / Sign up

Export Citation Format

Share Document