PMID- 23521535
OWN - NLM
STAT- MEDLINE
DCOM- 20131021
LR  - 20240514
IS  - 1520-510X (Electronic)
IS  - 0020-1669 (Print)
IS  - 0020-1669 (Linking)
VI  - 52
IP  - 8
DP  - 2013 Apr 15
TI  - Switching metal ion coordination and DNA Recognition in a Tandem CCHHC-type zinc 
      finger peptide.
PG  - 4721-8
LID - 10.1021/ic4003516 [doi]
AB  - Neural Zinc Finger Factor-1 (NZF-1) and Myelin Transcription Factor 1 (MyT1) are 
      two homologous nonclassical zinc finger (ZF) proteins that are involved in the 
      development of the central nervous system (CNS). Both NZF-1 and MyT1 contain 
      multiple ZF domains, each of which contains an absolutely conserved Cys2His2Cys 
      motif. All three cysteines and the second histidine have been shown to coordinate 
      Zn(II); however, the role of the first histidine remains unresolved. Using a 
      functional form of NZF-1 that contains two ZF domains (NZF-1-F2F3), mutant 
      proteins in which each histidine was sequentially mutated to a phenylalanine were 
      prepared to determine the role(s) of the histidine residues in DNA recognition. 
      When the first histidine is mutated, the protein binds Zn(II) in an analogous 
      manner to the native protein. Surprisingly, this mutant does not bind to target 
      DNA (beta-RAR), suggesting that the noncoordinating histidine is critical for 
      sequence selective DNA recognition. The first histidine will coordinate Zn(II) 
      when the second histidine is mutated; however, the overall fold of the protein is 
      perturbed leading to abrogation of DNA binding. NZF-1-F2F3 selectively binds to a 
      specific DNA target sequence (from beta-RAR) with high affinity (nM); while its 
      homologue MyT1 (MyT1-F2F3), which is 92% identical to NZF-1-F2F3, binds to this 
      same DNA sequence nonspecifically. A single, nonconserved amino acid residue in 
      NZF-1-F2F3 is shown to be responsible for this high affinity DNA binding to 
      beta-RAR. When this residue (arginine) is engineered into the MyT1-F2F3 sequence, 
      the affinity for beta-RAR DNA increases.
FAU - Besold, Angelique N
AU  - Besold AN
AD  - Department of Pharmaceutical Sciences, School of Pharmacy, University of 
      Maryland, Baltimore, Maryland 21201, United States.
FAU - Oluyadi, Abdulafeez A
AU  - Oluyadi AA
FAU - Michel, Sarah L J
AU  - Michel SL
LA  - eng
GR  - F31 NS074768/NS/NINDS NIH HHS/United States
GR  - F31NS074768/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20130322
PL  - United States
TA  - Inorg Chem
JT  - Inorganic chemistry
JID - 0366543
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Metals)
RN  - 0 (Myt1 protein, rat)
RN  - 0 (Myt1l protein, rat)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Peptides)
RN  - 0 (Trans-Activators)
RN  - 0 (Transcription Factors)
RN  - 3G0H8C9362 (Cobalt)
RN  - 4QD397987E (Histidine)
RN  - 9007-49-2 (DNA)
RN  - J41CSQ7QDS (Zinc)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Cobalt/metabolism
MH  - DNA/chemistry/*metabolism
MH  - DNA-Binding Proteins/chemistry/genetics/*metabolism
MH  - Histidine/chemistry/genetics/metabolism
MH  - Metals/*metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Nerve Tissue Proteins/chemistry/genetics/*metabolism
MH  - Peptides/*chemistry/genetics
MH  - Protein Binding
MH  - Rats
MH  - Sequence Alignment
MH  - Trans-Activators/chemistry/genetics/*metabolism
MH  - Transcription Factors/chemistry/genetics/*metabolism
MH  - Zinc/metabolism
MH  - *Zinc Fingers
PMC - PMC3671583
MID - NIHMS476460
EDAT- 2013/03/26 06:00
MHDA- 2013/10/22 06:00
PMCR- 2013/06/04
CRDT- 2013/03/26 06:00
PHST- 2013/03/26 06:00 [entrez]
PHST- 2013/03/26 06:00 [pubmed]
PHST- 2013/10/22 06:00 [medline]
PHST- 2013/06/04 00:00 [pmc-release]
AID - 10.1021/ic4003516 [doi]
PST - ppublish
SO  - Inorg Chem. 2013 Apr 15;52(8):4721-8. doi: 10.1021/ic4003516. Epub 2013 Mar 22.