Base sequence discrimination by zinc-finger DNA-binding domains

Nature ◽  
1991 ◽  
Vol 349 (6305) ◽  
pp. 175-178 ◽  
Author(s):  
Jeannette Nardelli ◽  
Toby J. Gibson ◽  
Christine Vesque ◽  
Patrick Charnay
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Base Sequence ◽  
Dna Binding Domains ◽  
Binding Domains

scholarly journals Artificial Zinc Finger DNA Binding Domains: Versatile Tools for Genome Engineering and Modulation of Gene Expression

2015 ◽  
Vol 116 (11) ◽  
pp. 2435-2444 ◽  
Author(s):  
Mir A. Hossain ◽  
Joeva J. Barrow ◽  
Yong Shen ◽  
MD Imdadul Haq ◽  
Jörg Bungert
Keyword(s):  
Gene Expression ◽  
Dna Binding ◽  
Zinc Finger ◽  
Genome Engineering ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Modulation Of Gene Expression

scholarly journals The Role of Zinc Finger Linkers in Zinc Finger Protein Binding to DNA

2020 ◽  
Author(s):  
Mazen Hamed ◽  
Reema Siam ◽  
Roza Zaid
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Zinc Finger ◽  
Zinc Finger Protein ◽  
Md Simulations ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Finger Protein ◽  
The Right

Zinc finger proteins (ZFP) play important roles in cellular processes. The DNA binding region of ZFP consists of 3 zinc finger DNA binding domains connected by amino acid linkers, the sequence TGQKP connects ZF1 and ZF2, and TGEKP connects ZF2 with ZF3. Linkers act to tune the zinc finger protein in the right position to bind its DNA target, the type of amino acid residues and length of linkers reflect on ZF1-ZF2-ZF3 interactions and contribute to the search and recognition process of ZF protein to its DNA target. Linker mutations and the affinity of the resulting mutants to specific and nonspecific DNA targets were studied by MD simulations and MM_GB(PB)SA. The affinity of mutants to DNA varied with type and position of amino acid residue. Mutation of K in TGQKP resulted in loss in affinity due to the loss of positive K interaction with phosphates, mutation of G showed loss in affinity to DNA, WT protein and all linker mutants showed loss in affinity to a nonspecific DNA target, this finding confirms previous reports which interpreted this loss in affinity as due to ZF1 having an anchoring role, and ZF3 playing an explorer role in the binding mechanism. The change in ZFP-DNA affinity with linker mutations is discussed in view of protein structure and role of linker residues in binding.

scholarly journals Male-specific Fruitless isoforms have different regulatory roles conferred by distinct zinc finger DNA binding domains

BMC Genomics ◽  
2013 ◽  
Vol 14 (1) ◽  
pp. 659 ◽  
Author(s):  
Justin E Dalton ◽  
Justin M Fear ◽  
Simon Knott ◽  
Bruce S Baker ◽  
Lauren M McIntyre ◽  
...  
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Male Specific

Developmentally Regulated Mouse Gene NK10 Encodes a Zinc Finger Repressor Protein with Differential DNA-Binding Domains

1995 ◽  
Vol 14 (11) ◽  
pp. 971-981 ◽  
Author(s):  
RITA LANGE ◽  
ANNETTE CHRISTOPH ◽  
HANS-JÜRGEN THIESEN ◽  
GABY VOPPER ◽  
KENNETH R. JOHNSON ◽  
...  
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Mouse Gene ◽  
Developmentally Regulated ◽  
Repressor Protein ◽  
Dna Binding Domains ◽  
Binding Domains

scholarly journals Characterization of the DNA-binding properties of the myeloid zinc finger protein MZF1: two independent DNA-binding domains recognize two DNA consensus sequences with a common G-rich core.

1994 ◽  
Vol 14 (3) ◽  
pp. 1786-1795 ◽  
Author(s):  
J F Morris ◽  
R Hromas ◽  
F J Rauscher
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Zinc Finger ◽  
Binding Sites ◽  
Zinc Fingers ◽  
Consensus Sequences ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Gel Shift ◽  
Myeloid Zinc Finger

The myeloid zinc finger gene 1, MZF1, encodes a transcription factor which is expressed in hematopoietic progenitor cells that are committed to myeloid lineage differentiation. MZF1 contains 13 C2H2 zinc fingers arranged in two domains which are separated by a short glycine- and proline-rich sequence. The first domain consists of zinc fingers 1 to 4, and the second domain is formed by zinc fingers 5 to 13. We have determined that both sets of zinc finger domains bind DNA. Purified, recombinant MZF1 proteins containing either the first set of zinc fingers or the second set were prepared and used to affinity select DNA sequences from a library of degenerate oligonucleotides by using successive rounds of gel shift followed by PCR amplification. Surprisingly, both DNA-binding domains of MZF1 selected similar DNA-binding consensus sequences containing a core of four or five guanine residues, reminiscent of an NF-kappa B half-site: 1-4, 5'-AGTGGGGA-3'; 5-13, 5'-CGGGnGAGGGGGAA-3'. The full-length MZF1 protein containing both sets of zinc finger DNA-binding domains recognizes synthetic oligonucleotides containing either the 1-4 or 5-13 consensus binding sites in gel shift assays. Thus, we have identified the core DNA consensus binding sites for each of the two DNA-binding domains of a myeloid-specific zinc finger transcription factor. Identification of these DNA-binding sites will allow us to identify target genes regulated by MZF1 and to assess the role of MZF1 as a transcriptional regulator of hematopoiesis.

scholarly journals The DNA binding domains of the yeast Ga14 and human c-Jun transcription factors interact through the zinc-finger and bZIP motifs

1995 ◽  
Vol 23 (4) ◽  
pp. 588-594 ◽  
Author(s):  
Kerstin Sollerbrant ◽  
Göran Akusjärvi ◽  
Stig Linder ◽  
Catharina Svensson
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Zinc Finger ◽  
Dna Binding Domains ◽  
Binding Domains

Engineered Cys2His2 zinc finger DNA-binding domains

2004 ◽  
Vol 2 (3) ◽  
pp. 191-206 ◽  
Author(s):  
Andrew S. Hirsh ◽  
J. Keith Joung
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Dna Binding Domains ◽  
Binding Domains
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