The SCAN Domain of ZNF174 Is a Dimer
The SCAN domain is a conserved region of 84 residues found predominantly in zinc finger DNA-binding proteins in vertebrates. The SCAN domain appears to control the association of SCAN domain containing proteins into noncovalent complexes and may be the primary mechanism underlying partner choice in...
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Published in | The Journal of biological chemistry Vol. 277; no. 7; pp. 5448 - 5452 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Society for Biochemistry and Molecular Biology
15.02.2002
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Subjects | |
Online Access | Get full text |
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Summary: | The SCAN domain is a conserved region of 84 residues found predominantly in zinc finger DNA-binding proteins in vertebrates.
The SCAN domain appears to control the association of SCAN domain containing proteins into noncovalent complexes and may be
the primary mechanism underlying partner choice in the oligomerization of these transcription factors. Here we have overexpressed,
purified, and characterized the isolated SCAN domain (amino acids 37â132) from ZNF174. Both size exclusion chromatography
and equilibrium sedimentation analysis demonstrate that the ZNF174 SCAN domain forms a homodimer. Circular dichroism shows
that the isolated SCAN domain dimer has â¼42% α-helix. Thermal denaturation experiments indicate that the SCAN domain undergoes
a single reversible unfolding transition with a T
m of over 70â°C. The midpoint of the equilibrium unfolding transition increases with increasing protein concentration, consistent
with a two-state unfolding transition in which folded dimer is in equilibrium with unfolded monomer. These findings demonstrate
that the isolated SCAN domain forms a stable dimer and support a model in which the SCAN domain is capable of mediating the
selective dimerization of a large family of vertebrate-specific, zinc finger-containing transcription factors. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.M109815200 |