scholarly journals Structures of Zinc Finger Domains from Transcription Factor Sp1

1997 ◽  
Vol 272 (12) ◽  
pp. 7801-7809 ◽  
Author(s):  
Vaibhav A. Narayan ◽  
Richard W. Kriwacki ◽  
John P. Caradonna
2001 ◽  
Vol 67 (1) ◽  
pp. 75-81 ◽  
Author(s):  
Jeffrey A. Rollins ◽  
Martin B. Dickman

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.


Author(s):  
Satoshi Yamanaka ◽  
Hidetaka Murai ◽  
Daisuke Saito ◽  
Gembu Abe ◽  
Etsuko Tokunaga ◽  
...  

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.


Genetics ◽  
1994 ◽  
Vol 138 (1) ◽  
pp. 125-134 ◽  
Author(s):  
M Hülskamp ◽  
W Lukowitz ◽  
A Beermann ◽  
G Glaser ◽  
D Tautz

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.


2010 ◽  
Vol 403 (2) ◽  
pp. 161-166 ◽  
Author(s):  
Tatsuo Ito ◽  
Haruka Kitamura ◽  
Chisana Uwatoko ◽  
Makiko Azumano ◽  
Kohji Itoh ◽  
...  

2009 ◽  
Vol 380 (1) ◽  
pp. 28-32 ◽  
Author(s):  
Tatsuo Ito ◽  
Makiko Azumano ◽  
Chisana Uwatoko ◽  
Kohji Itoh ◽  
Jun Kuwahara

2016 ◽  
Vol 45 (21) ◽  
pp. 8712-8716 ◽  
Author(s):  
Zhifeng Du ◽  
Raphael E. F. de Paiva ◽  
Yun Qu ◽  
Nicholas Farrell

The microenvironment around a zinc finger coordination unit affects the reactivity of apparently similar ZFs with Lewis acid platinum electrophiles. The unique dicysteine-bridged dinuclear platinum unit is the product of the reaction of [PtCl2(en)] and the F3 of the transcription factor Sp1.


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