Metal Ion Affinities of the Zinc Finger Domains of the Metal Responsive Element-Binding Transcription Factor-1 (MTF1)†

Biochemistry ◽  
2004 ◽  
Vol 43 (18) ◽  
pp. 5437-5444 ◽  
Author(s):  
Anthony L. Guerrerio ◽  
Jeremy M. Berg
Keyword(s):  
Transcription Factor ◽  
Zinc Finger ◽  
Metal Ion ◽  
Zinc Finger Domains ◽  
Responsive Element ◽  
Transcription Factor 1

scholarly journals pH Signaling in Sclerotinia sclerotiorum: Identification of a pacC/RIM1 Homolog

2001 ◽  
Vol 67 (1) ◽  
pp. 75-81 ◽  
Author(s):  
Jeffrey A. Rollins ◽  
Martin B. Dickman
Keyword(s):  
Transcription Factor ◽  
Oxalic Acid ◽  
Signaling Pathway ◽  
Zinc Finger ◽  
Sclerotinia Sclerotiorum ◽  
Culture Conditions ◽  
Phytopathogenic Fungi ◽  
Molecular Signaling ◽  
Ph Conditions ◽  
Zinc Finger Domains

ABSTRACT Sclerotinia sclerotiorum acidifies its ambient environment by producing oxalic acid. This production of oxalic acid during plant infection has been implicated as a primary determinant of pathogenicity in this and other phytopathogenic fungi. We found that ambient pH conditions affect multiple processes in S. sclerotiorum. Exposure to increasing alkaline ambient pH increased the oxalic acid accumulation independent of carbon source, sclerotial development was favored by acidic ambient pH conditions but inhibited by neutral ambient pH, and transcripts encoding the endopolygalacturonase gene pg1 accumulated maximally under acidic culture conditions. We cloned a putative transcription factor-encoding gene, pac1, that may participate in a molecular signaling pathway for regulating gene expression in response to ambient pH. The three zinc finger domains of the predicted Pac1 protein are similar in sequence and organization to the zinc finger domains of the A. nidulans pH-responsive transcription factor PacC. The promoter of pac1 contains eight PacC consensus binding sites, suggesting that this gene, like its homologs, is autoregulated. Consistent with this suggestion, the accumulation ofpac1 transcripts paralleled increases in ambient pH. Pac1 was determined to be a functional homolog of PacC by complementation of an A. nidulans pacC-null strain with pac1. Our results suggest that ambient pH is a regulatory cue for processes linked to pathogenicity, development, and virulence and that these processes may be under the molecular regulation of a conserved pH-dependent signaling pathway analogous to that in the nonpathogenic fungus A. nidulans.

scholarly journals PLZF is a new substrate of CRBN with thalidomide and 5-hydroxythalidomide

2020 ◽  
Author(s):  
Satoshi Yamanaka ◽  
Hidetaka Murai ◽  
Daisuke Saito ◽  
Gembu Abe ◽  
Etsuko Tokunaga ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Protein Synthesis ◽  
Zinc Finger ◽  
Cytochrome P450s ◽  
Synthesis System ◽  
Human Cytochrome ◽  
Zinc Finger Domains ◽  
Human Transcription Factor ◽  
Protein Synthesis System ◽  
Cell Free Protein Synthesis

AbstractThalidomide induces cereblon (CRBN)-dependent degradation of proteins. Human cytochrome P450s are thought to provide two monohydroxylated metabolites from thalidomide, and the metabolites are also considered to be involved in thalidomide effects. However, it remains unclear. We report that human PLZF/ZBTB16 is a target protein of CRBN with thalidomide and its derivatives, and that 5-hydroxythalidomide has high potential for degrading PLZF. Using a human transcription factor protein array produced by a wheat cell-free protein synthesis system, PLZF was found to bind to CRBN with thalidomide. PLZF is degraded by the CRL4CRBN complex with thalidomide and its derivatives. Mutagenesis analysis revealed that both 1st and 3rd zinc finger domains conserved in vertebrates are recognized for thalidomide-dependent binding and degradation by CRBN. In chicken limbs, knockdown of Plzf induced skeletal abnormalities, and Plzf was degraded after thalidomide or 5-hydroxythalidomide treatment. Our findings suggest that PLZF is a pivotal substrate involving thalidomide-induced teratogenesis.

scholarly journals Role of Metallothionein in Transcriptional Regulation by Metal-Responsive Element-Binding Transcription Factor 1

BPB Reports ◽  
2020 ◽  
Vol 3 (1) ◽  
pp. 22-27
Author(s):  
Yu-ki Tanaka ◽  
Yoshiaki Futami ◽  
Yasunori Fukumoto ◽  
Noriyuki Suzuki ◽  
Yasumitsu Ogra
Keyword(s):  
Transcription Factor ◽  
Transcriptional Regulation ◽  
Responsive Element ◽  
Transcription Factor 1

scholarly journals Differential regulation of target genes by different alleles of the segmentation gene hunchback in Drosophila.

Genetics ◽  
1994 ◽  
Vol 138 (1) ◽  
pp. 125-134 ◽  
Author(s):  
M Hülskamp ◽  
W Lukowitz ◽  
A Beermann ◽  
G Glaser ◽  
D Tautz
Keyword(s):  
Transcription Factor ◽  
Zinc Finger ◽  
Target Genes ◽  
Regulatory Gene ◽  
Differential Regulation ◽  
Coding Region ◽  
Segmentation Gene ◽  
Zinc Finger Domains ◽  
Morphogenetic Gradient ◽  
Blastoderm Stage

Abstract hunchback (hb) is a key regulatory gene in the early segmentation gene hierarchy of Drosophila. It codes for a transcription factor of the Cys2-His2 zinc finger type and shows two separate zinc finger domains in its coding region. hb forms a morphogenetic gradient in the middle of the embryo that is required for setting the spatial boundaries of several target genes. We have analyzed the molecular lesions found in the different hb alleles and have studied the differential effects of these alleles on a number of such target genes. We find that in mutants in which the HB protein lacks a functional second finger domain, the regulation of the target genes Krüppel (Kr) and knirps (kni) is differentially affected. While this domain is required for the correct regulation of Kr, it is not necessary for the repression of kni. Furthermore, mutations affecting this domain lead to a decreased protein stability. The integration of the expression pattern of target genes was found to be distorted in a second class of mutants between the two finger domains which lead to gain of function or neomorphic phenotypes. The effects of these mutations were studied in detail and it was found that they fall into two classes, the first one interfering with the function of the maternal hb product, the second leading to a delayed segmentation. The function of the latter class appears to be linked to the secondary expression of hb in the parasegment 4 (PS4) stripe at blastoderm stage.

scholarly journals Purification of proteins containing zinc finger domains using immobilized metal ion affinity chromatography

2011 ◽  
Vol 79 (1) ◽  
pp. 88-95 ◽  
Author(s):  
Irena Voráčková ◽  
Šárka Suchanová ◽  
Pavel Ulbrich ◽  
William E. Diehl ◽  
Tomáš Ruml
Keyword(s):  
Affinity Chromatography ◽  
Zinc Finger ◽  
Metal Ion ◽  
Zinc Finger Domains ◽  
Metal Ion Affinity Chromatography

scholarly journals Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV-Vis Spectroscopy

2017 ◽  
Vol 2017 ◽  
pp. 1-7 ◽  
Author(s):  
Valeria Sivo ◽  
Gianluca D’Abrosca ◽  
Luigi Russo ◽  
Rosa Iacovino ◽  
Paolo Vincenzo Pedone ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Coordination Sphere ◽  
Metal Ion ◽  
Electronic Configuration ◽  
Transition Band ◽  
Tetrahedral Geometry ◽  
Vis Spectroscopy ◽  
Zinc Finger Domains ◽  
Spectroscopic Probe

Co(II) electronic configuration allows its use as a spectroscopic probe in UV-Vis experiments to characterize the metal coordination sphere that is an essential component of the functional structure of zinc-binding proteins and to evaluate the metal ion affinities of these proteins. Here, exploiting the capability of the prokaryotic zinc finger to use different combinations of residues to properly coordinate the structural metal ion, we provide the UV-Vis characterization of Co(II) addition to Ros87 and its mutant Ros87_C27D which bears an unusual CysAspHis2 coordination sphere. Zinc finger sites containing only one cysteine have been infrequently characterized. We show for the CysAspHis2 coordination an intense d-d transition band, blue-shifted with respect to the Cys2His2 sphere. These data complemented by NMR and CD data demonstrate that the tetrahedral geometry of the metal site is retained also in the case of a single-cysteine coordination sphere.

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