Human p8 Is a HMG-I/Y-like Protein with DNA Binding Activity Enhanced by Phosphorylation
We have studied the biochemical features, the conformational preferences in solution, and the DNA binding properties of human p8 (hp8), a nucleoprotein whose expression is affected during acute pancreatitis. Biochemical studies show that hp8 has properties of the high mobility group proteins, HMG-I/...
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2001
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paper:paper_00219258_v276_n4_p2742_Encinar2023-06-08T14:43:20Z Human p8 Is a HMG-I/Y-like Protein with DNA Binding Activity Enhanced by Phosphorylation Mallo, Gustavo V. Mizyrycki, Cynthia L. Giono, Luciana Eugenia Cánepa, Eduardo Tomás Moreno de Colonna, Silvia Biochemistry DNA Electrophoresis Fourier transform infrared spectroscopy Nuclear magnetic resonance spectroscopy Gel shift analysis Proteins cyclic AMP dependent protein kinase DNA high mobility group B1 protein monomer nucleoprotein protein hp8 unclassified drug basic helix loop helix transcription factor DNA binding protein growth promotor high mobility group A1a protein high mobility group protein P8 protein, human transcription factor tumor protein acute pancreatitis article binding affinity biophysics circular dichroism gel mobility shift assay human infrared spectroscopy nuclear magnetic resonance spectroscopy priority journal protein conformation protein DNA binding protein folding protein phosphorylation protein secondary structure sequence analysis sequence homology structure analysis amino acid sequence comparative study genetics metabolism molecular genetics nuclear magnetic resonance nucleotide sequence phosphorylation protein binding protein tertiary structure Amino Acid Sequence Basic Helix-Loop-Helix Transcription Factors Circular Dichroism Conserved Sequence Cyclic AMP-Dependent Protein Kinases DNA-Binding Proteins Growth Substances High Mobility Group Proteins HMGA1a Protein Humans Molecular Sequence Data Neoplasm Proteins Nuclear Magnetic Resonance, Biomolecular Phosphorylation Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Spectroscopy, Fourier Transform Infrared Transcription Factors We have studied the biochemical features, the conformational preferences in solution, and the DNA binding properties of human p8 (hp8), a nucleoprotein whose expression is affected during acute pancreatitis. Biochemical studies show that hp8 has properties of the high mobility group proteins, HMG-I/Y. Structural studies have been carried out by using circular dichroism (near- and far-ultraviolet), Fourier transform infrared, and NMR spectroscopies. All the biophysical probes indicate that hp8 is monomeric (up to 1 mM concentration) and partially unfolded in solution. The protein seems to bind DNA weakly, as shown by electrophoretic gel shift studies. On the other hand, hp8 is a substrate for protein kinase A (PKA). The phosphorylated hp8 (PKAhp8) has a higher content of secondary structure than the nonphosphorylated protein, as concluded by Fourier transform infrared studies. PKAhp8 binds DNA strongly, as shown by the changes in circular dichroism spectra, and gel shift analysis. Thus, although there is not a high sequence homology with HMG-I/Y proteins, hp8 can be considered as a HMG-I/Y-like protein. Fil:Mallo, G.V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Mizyrycki, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Giono, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Cánepa, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Moreno, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2001 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v276_n4_p2742_Encinar http://hdl.handle.net/20.500.12110/paper_00219258_v276_n4_p2742_Encinar |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Biochemistry DNA Electrophoresis Fourier transform infrared spectroscopy Nuclear magnetic resonance spectroscopy Gel shift analysis Proteins cyclic AMP dependent protein kinase DNA high mobility group B1 protein monomer nucleoprotein protein hp8 unclassified drug basic helix loop helix transcription factor DNA binding protein growth promotor high mobility group A1a protein high mobility group protein P8 protein, human transcription factor tumor protein acute pancreatitis article binding affinity biophysics circular dichroism gel mobility shift assay human infrared spectroscopy nuclear magnetic resonance spectroscopy priority journal protein conformation protein DNA binding protein folding protein phosphorylation protein secondary structure sequence analysis sequence homology structure analysis amino acid sequence comparative study genetics metabolism molecular genetics nuclear magnetic resonance nucleotide sequence phosphorylation protein binding protein tertiary structure Amino Acid Sequence Basic Helix-Loop-Helix Transcription Factors Circular Dichroism Conserved Sequence Cyclic AMP-Dependent Protein Kinases DNA-Binding Proteins Growth Substances High Mobility Group Proteins HMGA1a Protein Humans Molecular Sequence Data Neoplasm Proteins Nuclear Magnetic Resonance, Biomolecular Phosphorylation Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Spectroscopy, Fourier Transform Infrared Transcription Factors |
| spellingShingle |
Biochemistry DNA Electrophoresis Fourier transform infrared spectroscopy Nuclear magnetic resonance spectroscopy Gel shift analysis Proteins cyclic AMP dependent protein kinase DNA high mobility group B1 protein monomer nucleoprotein protein hp8 unclassified drug basic helix loop helix transcription factor DNA binding protein growth promotor high mobility group A1a protein high mobility group protein P8 protein, human transcription factor tumor protein acute pancreatitis article binding affinity biophysics circular dichroism gel mobility shift assay human infrared spectroscopy nuclear magnetic resonance spectroscopy priority journal protein conformation protein DNA binding protein folding protein phosphorylation protein secondary structure sequence analysis sequence homology structure analysis amino acid sequence comparative study genetics metabolism molecular genetics nuclear magnetic resonance nucleotide sequence phosphorylation protein binding protein tertiary structure Amino Acid Sequence Basic Helix-Loop-Helix Transcription Factors Circular Dichroism Conserved Sequence Cyclic AMP-Dependent Protein Kinases DNA-Binding Proteins Growth Substances High Mobility Group Proteins HMGA1a Protein Humans Molecular Sequence Data Neoplasm Proteins Nuclear Magnetic Resonance, Biomolecular Phosphorylation Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Spectroscopy, Fourier Transform Infrared Transcription Factors Mallo, Gustavo V. Mizyrycki, Cynthia L. Giono, Luciana Eugenia Cánepa, Eduardo Tomás Moreno de Colonna, Silvia Human p8 Is a HMG-I/Y-like Protein with DNA Binding Activity Enhanced by Phosphorylation |
| topic_facet |
Biochemistry DNA Electrophoresis Fourier transform infrared spectroscopy Nuclear magnetic resonance spectroscopy Gel shift analysis Proteins cyclic AMP dependent protein kinase DNA high mobility group B1 protein monomer nucleoprotein protein hp8 unclassified drug basic helix loop helix transcription factor DNA binding protein growth promotor high mobility group A1a protein high mobility group protein P8 protein, human transcription factor tumor protein acute pancreatitis article binding affinity biophysics circular dichroism gel mobility shift assay human infrared spectroscopy nuclear magnetic resonance spectroscopy priority journal protein conformation protein DNA binding protein folding protein phosphorylation protein secondary structure sequence analysis sequence homology structure analysis amino acid sequence comparative study genetics metabolism molecular genetics nuclear magnetic resonance nucleotide sequence phosphorylation protein binding protein tertiary structure Amino Acid Sequence Basic Helix-Loop-Helix Transcription Factors Circular Dichroism Conserved Sequence Cyclic AMP-Dependent Protein Kinases DNA-Binding Proteins Growth Substances High Mobility Group Proteins HMGA1a Protein Humans Molecular Sequence Data Neoplasm Proteins Nuclear Magnetic Resonance, Biomolecular Phosphorylation Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Spectroscopy, Fourier Transform Infrared Transcription Factors |
| description |
We have studied the biochemical features, the conformational preferences in solution, and the DNA binding properties of human p8 (hp8), a nucleoprotein whose expression is affected during acute pancreatitis. Biochemical studies show that hp8 has properties of the high mobility group proteins, HMG-I/Y. Structural studies have been carried out by using circular dichroism (near- and far-ultraviolet), Fourier transform infrared, and NMR spectroscopies. All the biophysical probes indicate that hp8 is monomeric (up to 1 mM concentration) and partially unfolded in solution. The protein seems to bind DNA weakly, as shown by electrophoretic gel shift studies. On the other hand, hp8 is a substrate for protein kinase A (PKA). The phosphorylated hp8 (PKAhp8) has a higher content of secondary structure than the nonphosphorylated protein, as concluded by Fourier transform infrared studies. PKAhp8 binds DNA strongly, as shown by the changes in circular dichroism spectra, and gel shift analysis. Thus, although there is not a high sequence homology with HMG-I/Y proteins, hp8 can be considered as a HMG-I/Y-like protein. |
| author |
Mallo, Gustavo V. Mizyrycki, Cynthia L. Giono, Luciana Eugenia Cánepa, Eduardo Tomás Moreno de Colonna, Silvia |
| author_facet |
Mallo, Gustavo V. Mizyrycki, Cynthia L. Giono, Luciana Eugenia Cánepa, Eduardo Tomás Moreno de Colonna, Silvia |
| author_sort |
Mallo, Gustavo V. |
| title |
Human p8 Is a HMG-I/Y-like Protein with DNA Binding Activity Enhanced by Phosphorylation |
| title_short |
Human p8 Is a HMG-I/Y-like Protein with DNA Binding Activity Enhanced by Phosphorylation |
| title_full |
Human p8 Is a HMG-I/Y-like Protein with DNA Binding Activity Enhanced by Phosphorylation |
| title_fullStr |
Human p8 Is a HMG-I/Y-like Protein with DNA Binding Activity Enhanced by Phosphorylation |
| title_full_unstemmed |
Human p8 Is a HMG-I/Y-like Protein with DNA Binding Activity Enhanced by Phosphorylation |
| title_sort |
human p8 is a hmg-i/y-like protein with dna binding activity enhanced by phosphorylation |
| publishDate |
2001 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v276_n4_p2742_Encinar http://hdl.handle.net/20.500.12110/paper_00219258_v276_n4_p2742_Encinar |
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