Structure/function of KRAB repression domains: Structural properties of KRAB modules inferred from hydrodynamic, circular dichroism, and FTIR spectroscopic analyses
Keywords: Circular Dichroism, Ftir, Krab, Structural Content, Glutathione Transferase, Hybrid Protein, Transcription Factor, Transcription Factor Kap1, Transcription Factor Krip 1, Transcription Factor Tif1beta, Unclassified Drug, Zinc Finger Protein, Zinc Finger Protein 2 Kruppel Associated Box A, Article, Escherichia Coli, Expression Vector, Gel Filtration, Hydrodynamics, Hydrophobicity, Infrared Spectroscopy, Kruppel Associated Box Domain, Priority Journal, Protein Aggregation, Protein Assembly, Protein Denaturation, Protein Domain, Protein Expression, Protein Folding, Protein Function, Protein Motif, Protein Protein Interaction, Protein Purification, Protein Secondary Structure, Protein Structure, Sequence Analysis, Transcription Regulation, Ultraviolet Spectroscopy, Amino Acid Sequence, Binding Sites, Dna-Binding Proteins, Genetic Vectors, Humans, Kinetics, Models, Theoretical, Molecular Sequence Data, Recombinant Proteins, Repressor Proteins, Sequence Alignment, Sequence Homology, Solubility, Fourier Transform Infrared, Ultraviolet Rays, Erratum,
Affiliations: *** IBB - CNR ***
Istituto di Genetica e Biofisica Adriano Buzzati-Traverso, CNR, Napoli, Italy
Istituto di Biochimica delle Proteine, CNR, Napoli, Italy
Istituto di Scienze dell'Alimentazione, CNR, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy
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Bellefroid, E. J., Poncelet, D. A., Lecocq, P. J., Relevant, O., Martial, J. A., The evolutionarily conserved Kr ppel-associated box domain defines a subfamily of eukaryotic multifingered proteins (1991) Proc Natl Acad Sci USA, 88, pp. 3608-3612
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Uversky, V. N., What does it mean to be natively unfolded? (2002) Eur J Biochem, 269, pp. 2-12
Uversky, V. N., Gillespie, J. R., Fink, A. L., Why are "natively unfolded" proteins unstructured under physiologic conditions? (2000) Proteins, 41, pp. 415-427
Scir, A., Saccucci, F., Bertoli, E., Cambria, M. T., Principato, G., D'Auria, S., Tanfani, F., Effect of acidic phospholipids on the structural properties of recombinant cytosolic human glyoxalase II (2002) Proteins, 48, pp. 126-133
Arrondo, J. L., Muga, A., Castresana, J., Goni, F. M., Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy (1993) Prog Biophys Mol Biol, 59, pp. 23-56
Arrondo, J. L., Goni, F. M., Structure and dynamics of membrane proteins as studied by infrared spectroscopy (1999) Prog Biophys Mol Biol, 72, pp. 367-405
Brown, C. J., Takayama, S., Campen, A. M., Vise, P., Marshall, T. W., Oldfield, C. J., Williams, C. J., Dunker, A. K., Evolutionary rate heterogeneity in proteins with long disordered regions (2002) J Mol Evol, 55, pp. 104-110
Structure/function of KRAB repression domains: Structural properties of KRAB modules inferred from hydrodynamic, circular dichroism, and FTIR spectroscopic analyses
The abundant zinc finger proteins (ZFPs) sharing the KRAB motif, a potent transcription repression domain, direct the assembly on templates of multiprotein repression complexes. A pivotal step in this pathway is the assembly of a KRAB domain-directed complex with a primary corepressor, KAP1/KRIP-1/TIF1 beta. The structure/function dependence of KRAB/TIF1 beta protein-protein interaction and properties of the complex, therefore, play pivotal roles in diverse cellular processes depending on KRAB-ZFPs regulation. KRAB domains are functionally bipartite. The 42 amino acid-long KRAB-A module, indeed, is necessary and sufficient for transcriptional repression and for the interaction with the tripartite RBCC region of TIF1 beta, while the KRAB-B motif seems to potentiate the assembly of the complex. The structural properties of KRAB-A and KRAB-AB domains from the human ZNF2 protein have been investigated by characterizing highly purified lone (A) and composite (AB) modules. Hydrodynamic and spectroscopic features, investigated by means of gel filtration, circular dichroism, and infrared spectroscopy, provide evidence that both KRAB-A and KRAB-AB domains present low compactness, structural disorder, residual secondary structure content, flexibility, and tendency to molecular aggregation. Comparative analysis among KRAB-A and KRAB-AB modules suggests that the presence of the -B module may influence the properties of lone KRAB-A by affecting the structural flexibility and stability of the conformers. The combined experimental data and the intrinsic features of KRAB-A and KRAB-AB primary structures indicate a potential role of specific subregions within the modules in driving structural flexibility, which is proposed to be of importance for their function.
Structure/function of KRAB repression domains: Structural properties of KRAB modules inferred from hydrodynamic, circular dichroism, and FTIR spectroscopic analyses
Structure/function of KRAB repression domains: Structural properties of KRAB modules inferred from hydrodynamic, circular dichroism, and FTIR spectroscopic analyses
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