Alternating zinc fingers in the human male associated protein ZFY: 2D NMR structure of an even finger and implications for jumping-linker DNA recognition

Journal Article · Tue Apr 09 04:00:00 EDT 1991 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00228a004· OSTI ID:5464637

Kochoyan, M; Havel, T F; Dahl, C E ^[1]; Nguyen, D T; Keutmann, H T ^[2]; Weiss, M A ^[3]

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1. Harvard Medical School, Boston, MA (USA)
2. Massachusetts General Hospital, Boston, MA (USA)
3. Harvard Medical School, Boston, MA (USA) Massachusetts General Hospital, Boston (USA)

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, the authors have undertaken biochemical and structural studies of fragments of ZFY. They 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 HX{sub 4}HX{sub 3}-hydrophobic residue-X{sub 3}.

• OSTI ID: 5464637
• Journal Information: Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 30:14; ISSN 0006-2960; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
CHROMOSOMES
GENE REGULATION
HETEROCHROMOSOMES
HUMAN Y CHROMOSOME
MAGNETIC RESONANCE
MAMMALS
MAN
NUCLEAR MAGNETIC RESONANCE
NUCLEOPROTEINS
ORGANIC COMPOUNDS
PRIMATES
PROTEIN STRUCTURE
PROTEINS
RESONANCE
STRUCTURE-ACTIVITY RELATIONSHIPS
TRANSCRIPTION FACTORS
VERTEBRATES
Y CHROMOSOME