Linked Life Data

1849423

Source:http://linkedlifedata.com/resource/pubmed/id/1849423

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1991-5-13
pubmed:abstractText
ZFY, a sex-related Zn-finger protein encoded by the human Y chromosome, is distinguished from the general class of Zn-finger proteins by the presence of a two-finger repeat. Whereas odd-numbered domains and linkers fit a general consensus, even-numbered domains and linkers exhibit systematic differences. Because this alternation may have fundamental implications for the mechanism of protein-DNA recognition, we have undertaken biochemical and structural studies of fragments of ZFY. We describe here the solution structure of a representative nonconsensus (even-numbered) Zn finger based on 2D NMR studies of a 30-residue peptide. Structural modeling by distance geometry and simulated annealing (DG/SA) demonstrates that this peptide folds as a miniglobular domain containing a C-terminal beta--hairpin and N-terminal alpha-helix (beta beta alpha motif). These features are similar to (but not identical with) those previously described in consensus-type Zn fingers (derived from ADR1 and Xfin); the similarities suggest that even and odd ZFY domains bind DNA by a common mechanism. A model of the protein-DNA complex (designated the "jumping-linker" model) is presented and discussed in terms of the ZFY two-finger repeat. In this model every other linker is proposed to cross the minor groove by means of a putative finger/linker submotif HX4HX3-hydrophobic residue-X3. Analogous use of a hydrophobic residue in a linker that spans the minor groove has recently been described in crystallographic and 3D NMR studies of homeodomain-DNA complexes. The proposed model of ZFY is supported in part by the hydroxyl radical footprint of the TFIIIA-DNA complex [Churchill, M.E.A., Tullius, T.D., & Klug, A. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 5528-5532].
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3371-86
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:1849423-Amino Acid Sequence, pubmed-meshheading:1849423-Computer Graphics, pubmed-meshheading:1849423-DNA-Binding Proteins, pubmed-meshheading:1849423-Humans, pubmed-meshheading:1849423-Hydroxides, pubmed-meshheading:1849423-Hydroxyl Radical, pubmed-meshheading:1849423-Kruppel-Like Transcription Factors, pubmed-meshheading:1849423-Magnetic Resonance Spectroscopy, pubmed-meshheading:1849423-Male, pubmed-meshheading:1849423-Models, Molecular, pubmed-meshheading:1849423-Molecular Sequence Data, pubmed-meshheading:1849423-Nucleic Acid Conformation, pubmed-meshheading:1849423-Protein Conformation, pubmed-meshheading:1849423-Solubility, pubmed-meshheading:1849423-Spin Labels, pubmed-meshheading:1849423-Transcription Factor TFIIIA, pubmed-meshheading:1849423-Transcription Factors, pubmed-meshheading:1849423-Zinc, pubmed-meshheading:1849423-Zinc Fingers
pubmed:year
1991
pubmed:articleTitle
Alternating zinc fingers in the human male associated protein ZFY: 2D NMR structure of an even finger and implications for "jumping-linker" DNA recognition.
pubmed:affiliation
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't