Generation of monoclonal antibodies to the zinc finger domain of the eukaryotic transcription factor Sp1

1991 ◽  
Vol 101 (1) ◽  
Author(s):  
Hitoshi Katai ◽  
Kuniaki Terato ◽  
Rajendra Raghow
Keyword(s):  
Transcription Factor ◽  
Monoclonal Antibodies ◽  
Zinc Finger ◽  
Zinc Finger Domain ◽  
Eukaryotic Transcription ◽  
Transcription Factor Sp1

Interaction of Sp1 zinc finger with transport factor in the nuclear localization of transcription factor Sp1

2010 ◽  
Vol 403 (2) ◽  
pp. 161-166 ◽  
Author(s):  
Tatsuo Ito ◽  
Haruka Kitamura ◽  
Chisana Uwatoko ◽  
Makiko Azumano ◽  
Kohji Itoh ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Zinc Finger ◽  
Nuclear Localization ◽  
Transport Factor ◽  
Transcription Factor Sp1

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
Keyword(s):  
Transcription Factor ◽  
Zinc Finger ◽  
Transcription Factor Sp1 ◽  
Zinc Finger Domains

Role of zinc finger structure in nuclear localization of transcription factor Sp1

2009 ◽  
Vol 380 (1) ◽  
pp. 28-32 ◽  
Author(s):  
Tatsuo Ito ◽  
Makiko Azumano ◽  
Chisana Uwatoko ◽  
Kohji Itoh ◽  
Jun Kuwahara
Keyword(s):  
Transcription Factor ◽  
Zinc Finger ◽  
Nuclear Localization ◽  
Transcription Factor Sp1

scholarly journals Positional Cloning of Zinc Finger Domain Transcription Factor Zfp69, a Candidate Gene for Obesity-Associated Diabetes Contributed by Mouse Locus Nidd/SJL

PLoS Genetics ◽  
2009 ◽  
Vol 5 (7) ◽  
pp. e1000541 ◽  
Author(s):  
Stephan Scherneck ◽  
Matthias Nestler ◽  
Heike Vogel ◽  
Matthias Blüher ◽  
Marcel-Dominique Block ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Candidate Gene ◽  
Zinc Finger ◽  
Positional Cloning ◽  
Zinc Finger Domain

Tuning the reactivity of Sp1 zinc fingers with platinum complexes

2016 ◽  
Vol 45 (21) ◽  
pp. 8712-8716 ◽  
Author(s):  
Zhifeng Du ◽  
Raphael E. F. de Paiva ◽  
Yun Qu ◽  
Nicholas Farrell
Keyword(s):  
Transcription Factor ◽  
Zinc Finger ◽  
Lewis Acid ◽  
Zinc Fingers ◽  
Platinum Complexes ◽  
Coordination Unit ◽  
Transcription Factor Sp1 ◽  
Dinuclear Platinum

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.

Unique DNA Binding Mode of the N-Terminal Zinc Finger of Transcription Factor Sp1†

Biochemistry ◽  
1998 ◽  
Vol 37 (19) ◽  
pp. 6824-6832 ◽  
Author(s):  
Masanori Yokono ◽  
Nana Saegusa ◽  
Keizo Matsushita ◽  
Yukio Sugiura
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Zinc Finger ◽  
Binding Mode ◽  
Transcription Factor Sp1

scholarly journals Regulation of Transcription Factor YY1 by Acetylation and Deacetylation

2001 ◽  
Vol 21 (17) ◽  
pp. 5979-5991 ◽  
Author(s):  
Ya-Li Yao ◽  
Wen-Ming Yang ◽  
Edward Seto
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Zinc Finger ◽  
Binding Activity ◽  
Terminal Region ◽  
Histone Deacetylation ◽  
Regulation Of Transcription ◽  
Creb Binding Protein ◽  
Zinc Finger Domain ◽  
Histone Deacetylase 1

ABSTRACT YY1 is a sequence-specific DNA-binding transcription factor that has many important biological roles. It activates or represses many genes during cell growth and differentiation and is also required for the normal development of mammalian embryos. Previous studies have established that YY1 interacts with histone acetyltransferases p300 and CREB-binding protein (CBP) and histone deacetylase 1 (HDAC1), HDAC2, and HDAC3. Here, we present evidence that the activity of YY1 is regulated through acetylation by p300 and PCAF and through deacetylation by HDACs. YY1 was acetylated in two regions: both p300 and PCAF acetylated the central glycine-lysine-rich domain of residues 170 to 200, and PCAF also acetylated YY1 at the C-terminal DNA-binding zinc finger domain. Acetylation of the central region was required for the full transcriptional repressor activity of YY1 and targeted YY1 for active deacetylation by HDACs. However, the C-terminal region of YY1 could not be deacetylated. Rather, the acetylated C-terminal region interacted with HDACs, which resulted in stable HDAC activity associated with the YY1 protein. Finally, acetylation of the C-terminal zinc finger domain decreased the DNA-binding activity of YY1. Our findings suggest that in the natural context, YY1 activity is regulated through intricate mechanisms involving negative feedback loops, histone deacetylation, and recognition of the cognate DNA sequence affected by acetylation and deacetylation of the YY1 protein.

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