scholarly journals TATA Binding Proteins Can Recognize Nontraditional DNA Sequences

2012 ◽  
Vol 103 (7) ◽  
pp. 1510-1517 ◽  
Author(s):  
Sunmin Ahn ◽  
Chia-Ling Huang ◽  
Emre Ozkumur ◽  
Xirui Zhang ◽  
Jyothsna Chinnala ◽  
...  
Molecules ◽  
2018 ◽  
Vol 23 (11) ◽  
pp. 2748 ◽  
Author(s):  
Ae-Ree Lee ◽  
Na-Hyun Kim ◽  
Yeo-Jin Seo ◽  
Seo-Ree Choi ◽  
Joon-Hwa Lee

Z-DNA is stabilized by various Z-DNA binding proteins (ZBPs) that play important roles in RNA editing, innate immune response, and viral infection. In this review, the structural and dynamics of various ZBPs complexed with Z-DNA are summarized to better understand the mechanisms by which ZBPs selectively recognize d(CG)-repeat DNA sequences in genomic DNA and efficiently convert them to left-handed Z-DNA to achieve their biological function. The intermolecular interaction of ZBPs with Z-DNA strands is mediated through a single continuous recognition surface which consists of an α3 helix and a β-hairpin. In the ZBP-Z-DNA complexes, three identical, conserved residues (N173, Y177, and W195 in the Zα domain of human ADAR1) play central roles in the interaction with Z-DNA. ZBPs convert a 6-base DNA pair to a Z-form helix via the B-Z transition mechanism in which the ZBP first binds to B-DNA and then shifts the equilibrium from B-DNA to Z-DNA, a conformation that is then selectively stabilized by the additional binding of a second ZBP molecule. During B-Z transition, ZBPs selectively recognize the alternating d(CG)n sequence and convert it to a Z-form helix in long genomic DNA through multiple sequence discrimination steps. In addition, the intermediate complex formed by ZBPs and B-DNA, which is modulated by varying conditions, determines the degree of B-Z transition.


1992 ◽  
Vol 287 (2) ◽  
pp. 349-353 ◽  
Author(s):  
T Yoganathan ◽  
N K Bhat ◽  
B H Sells

The beta factor, which interacts with the rpL32 promoter, binds to the sequence 5′-GAGCCGGAAGTG and trans-activates this gene. Comparison of the DNA sequences bound by the beta factor with those bound by other known DNA-binding proteins revealed that the ETS proteins interact with similar DNA sequences. Consequently we have examined the relationship of the beta factor to the several ETS proteins so far reported. Antibody and oligonucleotide competition experiments, performed by using electrophoretic shift analysis, revealed that the beta factor contains ETS epitopes and that it is immunologically related to both of the GA-binding proteins (GABPs), implying that the beta factor may consist of two separate protein subunits.


Biochemistry ◽  
1999 ◽  
Vol 38 (35) ◽  
pp. 11340-11348 ◽  
Author(s):  
Amy J. Jackson-Fisher ◽  
Sandeep Burma ◽  
Matthew Portnoy ◽  
Lumelle A. Schneeweis ◽  
Robert A. Coleman ◽  
...  

1990 ◽  
Vol 56 (2-3) ◽  
pp. 115-120 ◽  
Author(s):  
Susumu Ohno

SummaryRegardless of their origins, functions, and base compositions, all DNAs are scriptures written following the same grammatical rule. At the level of syllables, two, CG and TA are seldom used, while three, TG, CT and CA are utilized with abundance. Accordingly, at the level of three-letter words, two complementary base trimers, CTG and CAG, invariably enjoy frequent usage. Inasmuch as two of the three frequently used syllables, TG and CA are complementary to each other, while two seldom used syllables, CG and TA, are both palindromes, two complementary strands of DNA are inherently symmetrical with each other. Consequently, palindromic sequences as favourite targets of DNA-binding proteins occur at unsuspectedly high frequencies, if they contain TG and CA or CTG and CAG. Nevertheless, there are grammatical rules operating among these high frequency palindromes as well; e.g. the palindromic tetramer TGCA occurs nearly two times more often than its reciprocal; CATG. Thus, DNA-binding proteins are provided with a wealth of abundant targets whose densities are influenced by a regional difference in GC/AT ratios to variable degrees. One palindromic heptamer CAGNCTG is an ideal target of one DNA-binding protein engaged in chromosome packaging and in generation of banding patterns. This heptamer occurs once every 1000 bases in moderately GC-rich sequences, while its incidence is reduced to once every 3000 bases in extremely AT-rich sequences. The above must be the very reason that a solitary human X-chromosome DNA coated with mouse DNA-binding proteins in mouse-man somatic hybrids still maintains the original banding pattern and that the inactive X remains inactive, while the active X remains active.


Genetics ◽  
2020 ◽  
Vol 214 (3) ◽  
pp. 623-634
Author(s):  
Elnaz Ghotbi ◽  
Kristina Lackey ◽  
Vicki Wong ◽  
Katie T. Thompson ◽  
Evan G. Caston ◽  
...  

Polycomb-group (PcG) proteins are evolutionarily conserved epigenetic regulators whose primary function is to maintain the transcriptional repression of target genes. Recruitment of Drosophila melanogaster PcG proteins to target genes requires the presence of one or more Polycomb Response Elements (PREs). The functions or necessity for more than one PRE at a gene are not clear and individual PREs at some loci may have distinct regulatory roles. Various combinations of sequence-specific DNA-binding proteins are present at a given PRE, but only Pleiohomeotic (Pho) is present at all strong PREs. The giant (gt) locus has two PREs, a proximal PRE1 and a distal PRE2. During early embryonic development, Pho binds to PRE1 ∼30-min prior to stable binding to PRE2. This observation indicated a possible dependence of PRE2 on PRE1 for PcG recruitment; however, we find here that PRE2 recruits PcG proteins and maintains transcriptional repression independently of Pho binding to PRE1. Pho-like (Phol) is partially redundant with Pho during larval development and binds to the same DNA sequences in vitro. Although binding of Pho to PRE1 is dependent on the presence of consensus Pho-Phol-binding sites, Phol binding is less so and appears to play a minimal role in recruiting other PcG proteins to gt. Another PRE-binding protein, Sp1/Kruppel-like factor, is dependent on the presence of Pho for PRE1 binding. Further, we show that, in addition to silencing gene expression, PcG proteins dampen transcription of an active gene.


PLoS ONE ◽  
2012 ◽  
Vol 7 (2) ◽  
pp. e30446 ◽  
Author(s):  
Chien-Yu Chen ◽  
Ting-Ying Chien ◽  
Chih-Kang Lin ◽  
Chih-Wei Lin ◽  
Yi-Zhong Weng ◽  
...  

2016 ◽  
Vol 18 (16) ◽  
pp. 11184-11192 ◽  
Author(s):  
David Gomez ◽  
Stefan Klumpp

Recognition of specific DNA sequences by DNA-binding proteins (DBPs) takes place by a facilitated diffusion process that depends, among other parameters, on the DBP's sliding length on the DNA and the DNA concentration. In addition, facilitated diffusion is variously impaired by the presence of obstacles with different dynamics on the DNA.


1994 ◽  
Vol 8 (11) ◽  
pp. 1335-1343 ◽  
Author(s):  
B P Cormack ◽  
M Strubin ◽  
L A Stargell ◽  
K Struhl

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