PMID- 20229093
OWN - NLM
STAT- MEDLINE
DCOM- 20100701
LR  - 20181113
IS  - 1432-1327 (Electronic)
IS  - 0949-8257 (Linking)
VI  - 15
IP  - 4
DP  - 2010 May
TI  - Functional characterization of iron-substituted neural zinc finger factor 1: 
      metal and DNA binding.
PG  - 583-90
LID - 10.1007/s00775-010-0626-1 [doi]
AB  - Neural zinc finger factor 1 (NZF-1) is a nonclassical zinc finger protein 
      involved in neuronal development. NZF-1 contains multiple copies of a unique 
      CCHHC zinc-binding domain that recognize a promoter element in the beta-retinoic 
      acid receptor gene termed beta-retinoic acid receptor element (beta-RARE). 
      Previous studies have established that a two-domain fragment of NZF-1 bound with 
      zinc is sufficient for specific DNA binding. Proper functioning of the nervous 
      system relies heavily on iron and misregulation of this highly redox active metal 
      has serious consequences. Several classes of zinc finger proteins have been shown 
      to bind other metal ions, including iron. To determine if ferrous iron can 
      coordinate to the metal-binding sites of NZF-1 and assess the functional 
      consequences of such coordination, a fragment of NZF-1 that contains two 
      zinc-binding domains, NZF-1 double finger (NZF-1-DF), was prepared. UV-vis 
      spectroscopy experiments demonstrated that Fe(II) is capable of binding to 
      NZF-1-DF. Upon reconstitution with either Fe(II) or Zn(II), NZF-1-DF binds 
      selectively and tightly (nanomolar affinity) to its target beta-RARE DNA 
      sequence, whereas apo-NZF-1-DF does not bind to DNA and instead aggregates.
FAU - Besold, Angelique N
AU  - Besold AN
AD  - Department of Pharmaceutical Sciences, School of Pharmacy, University of 
      Maryland, Baltimore, MD 21201, USA.
FAU - Lee, Seung Jae
AU  - Lee SJ
FAU - Michel, Sarah L J
AU  - Michel SL
FAU - Sue, Niall Lue
AU  - Sue NL
FAU - Cymet, Holly J
AU  - Cymet HJ
LA  - eng
GR  - 5 G12RR017581-03/RR/NCRR 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 - 20100313
PL  - Germany
TA  - J Biol Inorg Chem
JT  - Journal of biological inorganic chemistry : JBIC : a publication of the Society 
      of Biological Inorganic Chemistry
JID - 9616326
RN  - 0 (Apoproteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Peptide Fragments)
RN  - 789U1901C5 (Copper)
RN  - 9007-49-2 (DNA)
RN  - E1UOL152H7 (Iron)
SB  - IM
MH  - Air
MH  - Amino Acid Sequence
MH  - Apoproteins/chemistry/metabolism
MH  - Base Sequence
MH  - Copper/metabolism
MH  - DNA/genetics/*metabolism
MH  - *Iron
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/*chemistry/*metabolism
MH  - Oxidation-Reduction
MH  - Peptide Fragments/chemistry/metabolism
MH  - Promoter Regions, Genetic/genetics
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Spectrophotometry, Ultraviolet
MH  - Substrate Specificity
EDAT- 2010/03/17 06:00
MHDA- 2010/07/02 06:00
CRDT- 2010/03/16 06:00
PHST- 2009/07/13 00:00 [received]
PHST- 2010/01/20 00:00 [accepted]
PHST- 2010/03/16 06:00 [entrez]
PHST- 2010/03/17 06:00 [pubmed]
PHST- 2010/07/02 06:00 [medline]
AID - 10.1007/s00775-010-0626-1 [doi]
PST - ppublish
SO  - J Biol Inorg Chem. 2010 May;15(4):583-90. doi: 10.1007/s00775-010-0626-1. Epub 
      2010 Mar 13.