In transcription factors

The general topology of rubredoxins is also observed in the general zinc-ribbon motif in RNA polymerases or in transcription factors (59). The first published zinc-ribbon structure was that of the nucleic-acid binding domain of human transcriptional elongation factor TFIIS (PDB file ITFI) 40). These zinc binding domains and rubredoxins... 

Several different classes of DNA-binding domains have been identified in transcription factors. 

The tetrahedron of zinc thiolates is found in enzymes in both cell types but is most frequently seen in transcription factors, zinc fingers of eukaryotes. 

Oxidised) organic molecules oxidation using iron but most notably copper zinc in transcription factors and hydrolytic enzymes (Chapter 8). 

Kurten S, Obe, G (1975) Premature chromosome condensation in the bone marrow of Chinese hamster after pUcation of bleomycin in vivo. Mutat Res 27(2) 285—294 Lee DY, Hayes JJ, Pruss D, Wolffe AP (1993) A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell 72 73—84... 

Figure 1. MARs serve to enrich the nuclear milieu by bringing in transcription factors and enzymes to regulate transcription...

The role of zinc in transcription factor IIIA is presumably structural, not catalytic, and is required for DNA-binding activity (Hanas et al.. 

DNA binding domains called basic domains (rich in basic amino acids), occur in transcription factors in combination with leucine zipper or helix-loop-helix (HLH) dimerization domains (see below). The combination of basic domain and dimerization domain gives these proteins their names of basic leucine zipper proteins (bZIP) or basic HLH proteins, respectively. In each case the dimerization means that two basic domains (one from each monomer) interact with the target DNA. 

The helix-loop-helix (HLH) dimerization domain is quite distinct from the helix-turn-helix motif described above (which is involved in DNA binding not dimerization) and must not be confused with it. The HLH domain consists of two a-helices separated by a nonhelical loop. The C-terminal a-helix has hydrophobic amino acids on one face. Thus two transcription factor monomers, each with an HLH motif, can dimerize by interaction between the hydrophobic faces of the two C-terminal a-helices. Like the leucine zipper (see above), the HLH motif is often found in transcription factors that contain basic DNA binding domains. Again, like the leucine zipper, the HLH motif can dimerize transcription factor monomers to form either homodimers or heterodimers. This ability to form heterodimers markedly increases the variety of active transcription factors that are possible and so increases the potential for gene regulation. 

Crabtree, G. R., Aebersold, R., Geoudine, M. (2004). Dynamic changes in transcription factor complexes during erythroid differentiation revealed by quantitative proteomics. Nat. Struct. 

Domain involved in protein-protein interaction, originally described in transcription factors LINl, ISLl, and MED3 Long interspersed nuclear element Liquid-liquid extraction Lower limit of detection Lower limit of quantification Large nuclear ribonucleoprotein Limit of detection logjo of odds... 

Chronic cocaine exposure and long-term adaptation at the molecular level have been investigated changes in transcription factor gene expression may be involved... 

Suzuki, M. (1994) A framework for the DNA-protein recognition code of the probe helix in transcription factors The chemical and stereochemical rules. Structure 2, 317-326. 

Moses, A. M., Chiang, D. Y., Kellis, M., Lander, E. S., and Eisen, M. B. (2003) Position specific variation in the rate of evolution in transcription factor binding sites. BMC Evol. Biol. 3, 19. 

What underlies transcriptional dysregulation In the case of PD, mutations in transcriptional factors themselves are an emerging theme. Two recent genetic association studies in a screening sample of large cohorts of individuals with idiopathic PD have revealed evidence for a novel association of PITX3 promoter... 

There are at least two SNPs (boxed in Figure 9.5) in the dbSNP track that are present in the 3 -UTR and could have functional significance. Since the coding polymorphisms in CAR are rare (Table 9.3), CAR hepatic expression shows 200-fold interindividual variation the variation in CAR may be due to either sequence variations 5 or 3 to the CAR coding region, or may be due to nucleotide variation in transcription factors regulating CAR. 

Activation and repression domains in transcription factors exhibit a variety of amino acid sequences and three-dimensional structures. In general, these functional do-... 

STATSa is a transcription factor that regulates the expression of cyclin D, BcI-Xl, and other genes. Why is it possible for these carcinomas that no mutation occurs in the cyclin D gene despite its overexpression Why are mutations in transcription-factor genes like STATSa commonly found in cancer cells ... 

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