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ZINC FINGER TRANSCRIPTION FACTORS IN SKELETAL DEVELOPMENT

CIHR Group in Matrix Dymanics, Faculty of Dentistry, University of Toronto, 239-150 College Street, Toronto, ON M5S 3E2, Canada;

View larger version (17K): [in a new window]   Figure 1. A simplistic view of regulatory mechanisms of gene transcription. The RNA-transcribing enzyme, RNA polymerase II (red), requires general transcription factors (TFII) D, A, B, F, E, and H (blue), which themselves consist of multiple subunits, to recognize the transcription start site via the TATA box or related sequences in the core promoter. The sum of these factors, known as the pre-initiation complex (PIC), is required for basal transcription. Transcription factors (green) bind to specific DNA sequences (red) via their DNA-binding domain (DBD) and modulate the rate of transcription via their transactivation domain(s) (TAD).

View larger version (58K): [in a new window]   Figure 2. Genome-wide comparison of transcription factor families in eukaryotes. The relative sizes of the transcription factor families, categorized according to their DNA-binding domain, among Homo sapiens, Drosophila melanogaster, Caenorhabditis elegans, and Saccharomyces cerevisiae are indicated. Data are derived from an analysis of eukaryotic proteomes according to the INTERPRO database, which incorporates Pfam, PRINTS, and Prosite. The transcription factor families shown are the largest in their category out of the 1502 protein families listed by Integrated ProteomicsTM Inc. (IPI). Reproduced with permission from Tupler et al.(2001).

View larger version (39K): [in a new window]   Figure 3. C2H2 zinc finger motif. (A) The C2H2 zinc finger motif (2 Cys and 2 His residues bonded tetrahedrally to a Zn ion) consists of a short antiparallel ß-sheet formed by two ß-strands and hairpin turn, followed by an -helix (adapted from Lee et al., 1989). (B) Co-crystal structure of Zif268/DNA as determined by Pavletich and Pabo (1993). Note the -helices wrapped around the major groove of the DNA. N denotes the N-terminus. (C) ß-strands (arrows) and hairpin turn (curved line), followed by an -helix (blue helix) that usually fits into the major groove of the target DNA. Conserved amino acids are underlined. Amino acids (red) at positions –1, +3, and +6 relative to the beginning of the -helix are primarily responsible for interactions with DNA.

View larger version (43K): [in a new window]   Figure 4. Phenotype of osterix (Sp7)-deficient mice. Staining of skeletal preparations from embryonic day 15.5 (E15.5) and newborn homozygous mutant mice with alcian blue and alizarin red indicated a virtual absence of mineralization in all facial and skull bones formed by intramembranous ossification and a general deficiency of osteoblast differentiation. Reproduced with permission from Nakashima et al.(2002).