PMID- 10606515
OWN - NLM
STAT- MEDLINE
DCOM- 20000119
LR  - 20200401
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 38
IP  - 51
DP  - 1999 Dec 21
TI  - Metal and DNA binding properties of a two-domain fragment of neural zinc finger 
      factor 1, a CCHC-type zinc binding protein.
PG  - 16826-30
AB  - Neural zinc finger factor 1 (NZF-1) is a member of a family of neural-specific 
      transcription factors that contain multiple copies of a relatively 
      uncharacterized zinc binding motif. We have studied the metal binding and DNA 
      binding properties of a fragment of NZF-1 containing two adjacent zinc binding 
      domains. Partial proteolysis with endoproteinase Lys-C identified 
      metal-stabilized fragments containing either one or both of the zinc binding 
      domains. Both domains were required for specific DNA binding to the beta-retinoic 
      acid receptor element, producing a DNase I footprint covering predominantly one 
      strand. The metal binding site was probed via cobalt(II) substitution. The 
      visible absorption spectrum of the cobalt(II) complex is consistent with 
      Cys-Cys-His-Cys coordination of the metal. The two domains appear to have similar 
      affinities for metal and bind cobalt(II) and zinc(II) with dissociation constants 
      of 4 (+/- 2) x 10(-)(7) M and 1.4 (+/- 0.8) x 10(-)(10) M, respectively. The 
      domains fold upon the addition of zinc, as observed by (1)H NMR. However, an 
      additional weak binding site causes line broadening in the presence of excess 
      zinc, presumably due to aggregation.
FAU - Berkovits, H J
AU  - Berkovits HJ
AD  - Department of Biophysics and Biophysical Chemistry, The Johns Hopkins University 
      School of Medicine, Baltimore, Maryland 21205, USA.
FAU - Berg, J M
AU  - Berg JM
LA  - eng
GR  - GM 46257/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Myt1l protein, rat)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Trans-Activators)
RN  - 0 (retinoic acid receptor beta)
RN  - 3G0H8C9362 (Cobalt)
RN  - EC 3.1.21.1 (Deoxyribonuclease I)
RN  - J41CSQ7QDS (Zinc)
SB  - IM
MH  - Animals
MH  - Binding Sites/genetics
MH  - Cloning, Molecular
MH  - Cobalt/chemistry/metabolism
MH  - DNA Footprinting
MH  - DNA-Binding Proteins/*chemistry/genetics/metabolism
MH  - Deoxyribonuclease I/chemistry
MH  - Hydrolysis
MH  - Nerve Tissue Proteins/*chemistry/genetics/metabolism
MH  - Nuclear Magnetic Resonance, Biomolecular
MH  - Peptide Fragments/chemistry/genetics/isolation & purification/metabolism
MH  - Protein Folding
MH  - Protein Structure, Tertiary/genetics
MH  - Rats
MH  - Receptors, Retinoic Acid/genetics
MH  - Response Elements
MH  - Trans-Activators/*chemistry/genetics/metabolism
MH  - Zinc/*chemistry/metabolism
MH  - *Zinc Fingers/genetics
EDAT- 1999/12/22 00:00
MHDA- 1999/12/22 00:01
CRDT- 1999/12/22 00:00
PHST- 1999/12/22 00:00 [pubmed]
PHST- 1999/12/22 00:01 [medline]
PHST- 1999/12/22 00:00 [entrez]
AID - bi991433l [pii]
AID - 10.1021/bi991433l [doi]
PST - ppublish
SO  - Biochemistry. 1999 Dec 21;38(51):16826-30. doi: 10.1021/bi991433l.