Getting a grip on DNA recognition: structures of the basic region leucine zipper, and the basic region helix-loop-helix DNA-binding domains

1994 ◽  
Vol 4 (1) ◽  
pp. 12-21 ◽  
Author(s):  
Tom Ellenberger
Keyword(s):  
Dna Binding ◽  
Leucine Zipper ◽  
Dna Recognition ◽  
Dna Binding Domains ◽  
Helix Loop Helix ◽  
Binding Domains ◽  
Basic Region

scholarly journals Differential Gene Regulation by Selective Association of Transcriptional Coactivators and bZIP DNA-Binding Domains

2006 ◽  
Vol 26 (16) ◽  
pp. 5969-5982 ◽  
Author(s):  
Benoit Miotto ◽  
Kevin Struhl
Keyword(s):  
Dna Binding ◽  
Regulation Of Gene Expression ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Transcriptional Coactivators ◽  
Differential Gene Regulation ◽  
Arginine Residues ◽  
Contact Dna ◽  
Bzip Proteins ◽  
Basic Region

ABSTRACT bZIP DNA-binding domains are targets for viral and cellular proteins that function as transcriptional coactivators. Here, we show that MBF1 and the related Chameau and HBO1 histone acetylases interact with distinct subgroups of bZIP proteins, whereas pX does not discriminate. Selectivity of Chameau and MBF1 for bZIP proteins is mediated by residues in the basic region that lie on the opposite surface from residues that contact DNA. Chameau functions as a specific coactivator for the AP-1 class of bZIP proteins via two arginine residues. A conserved glutamic acid/glutamine in the linker region underlies MBF1 specificity for a subgroup of bZIP factors. Chameau and MBF1 cannot synergistically coactivate transcription due to competitive interactions with the basic region, but either protein can synergistically coactivate with pX. Analysis of Jun derivatives that selectively interact with these coactivators reveals that MBF1 is crucial for the response to oxidative stress, whereas Chameau is important for the response to chemical and osmotic stress. Thus, the bZIP domain mediates selective interactions with coactivators and hence differential regulation of gene expression.

FGF inactivates myogenic helix-loop-helix proteins through phosphorylation of a conserved protein kinase C site in their DNA-binding domains

Cell ◽  
1992 ◽  
Vol 71 (7) ◽  
pp. 1181-1194 ◽  
Author(s):  
Li Li ◽  
Jumin Zhou ◽  
Guy James ◽  
Robin Heller-Harrison ◽  
Michael P. Czech ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Dna Binding ◽  
Dna Binding Domains ◽  
Helix Loop Helix ◽  
Binding Domains ◽  
Kinase C

Modulation of DNA-binding domains for sequence-specific DNA recognition

Gene ◽  
2003 ◽  
Vol 304 ◽  
pp. 1-12 ◽  
Author(s):  
Ronen Marmorstein ◽  
Mary X. Fitzgerald
Keyword(s):  
Dna Binding ◽  
Dna Recognition ◽  
Dna Binding Domains ◽  
Binding Domains

CRITERIA FOR AN UPDATED CLASSIFICATION OF HUMAN TRANSCRIPTION FACTOR DNA-BINDING DOMAINS

2013 ◽  
Vol 11 (01) ◽  
pp. 1340007 ◽  
Author(s):  
EDGAR WINGENDER
Keyword(s):  
Dna Binding ◽  
Leucine Zipper ◽  
Regulatory Elements ◽  
Biological Species ◽  
Basic Leucine Zipper ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Comprehensive Classification ◽  
Human Transcription Factor

By binding to cis-regulatory elements in a sequence-specific manner, transcription factors regulate the activity of nearby genes. Here, we discuss the criteria for a comprehensive classification of human TFs based on their DNA-binding domains. In particular, classification of basic leucine zipper (bZIP) and zinc finger factors is exemplarily discussed. The resulting classification can be used as a template for TFs of other biological species.

scholarly journals Modular construction of extended DNA recognition surfaces: mutant DNA-binding domains of the 434 repressor as building blocks

2001 ◽  
Vol 14 (8) ◽  
pp. 591-599 ◽  
Author(s):  
Tiebing Liang ◽  
Jinqiu Chen ◽  
Marie-Louise Tjörnhammar ◽  
Sándor Pongor ◽  
András Simoncsits
Keyword(s):  
Dna Binding ◽  
Dna Recognition ◽  
Building Blocks ◽  
Modular Construction ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
434 Repressor

scholarly journals Domains of human c-myc protein required for autosuppression and cooperation with ras oncogenes are overlapping.

1990 ◽  
Vol 10 (9) ◽  
pp. 4961-4966 ◽  
Author(s):  
L J Penn ◽  
M W Brooks ◽  
E M Laufer ◽  
T D Littlewood ◽  
J P Morgenstern ◽  
...  
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Gene Transcription ◽  
Leucine Zipper ◽  
Rat Embryo ◽  
Helix Loop Helix ◽  
Myc Gene ◽  
Ras Oncogenes ◽  
Carboxyl Terminal ◽  
Basic Region

Amino acids 106 to 143 and 354 to 433 of the human c-myc protein (439 amino acids) were shown to be required for the protein to suppress c-myc gene transcription and were found to exactly overlap with those necessary for c-myc to cooperate with ras oncogenes in the transformation of rat embryo fibroblasts. The essential carboxyl-terminal region harbors structural motifs (a basic region, a helix-loop-helix motif, and a "leucine zipper"), which, in other proteins, can mediate dimerization and sequence-specific DNA binding.

Model-Building of Fnr and FixK DNA-binding domains suggests a basis for specific DNA recognition

1989 ◽  
Vol 2 (3) ◽  
pp. 114-121 ◽  
Author(s):  
Jacqueline Cherfils ◽  
Jean-François Gibrat ◽  
Jonathan Levin ◽  
Jacques Batut ◽  
Daniel Kahn
Keyword(s):  
Dna Binding ◽  
Model Building ◽  
Dna Recognition ◽  
Dna Binding Domains ◽  
Binding Domains
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