Ion channels formed by transcription factors recognize consensus DNA sequences
Transcription factors (TFs) are proteins which bind to specific DNA sequences and thus participate in the regulation of the initiation of transcription. We report in this communication our observations that several of these proteins interact with lipid membranes and form ion-permeable channels. For...
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2001
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1510_n1-2_p209_Tosteson http://hdl.handle.net/20.500.12110/paper_00052736_v1510_n1-2_p209_Tosteson |
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paper:paper_00052736_v1510_n1-2_p209_Tosteson |
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paper:paper_00052736_v1510_n1-2_p209_Tosteson2023-06-08T14:29:49Z Ion channels formed by transcription factors recognize consensus DNA sequences DNA binding Lipid bilayer Protein channel Transcription factor double stranded DNA ion channel transcription factor article consensus sequence DNA binding DNA sequence membrane binding membrane conductance priority journal protein lipid interaction Consensus Sequence Dimerization DNA Ion Channels Lipid Bilayers Membrane Potentials Molecular Conformation Protein Binding Transcription Factors Transcription factors (TFs) are proteins which bind to specific DNA sequences and thus participate in the regulation of the initiation of transcription. We report in this communication our observations that several of these proteins interact with lipid membranes and form ion-permeable channels. For each of the TFs that we studied, the single channel conductance was distinctively different, i.e. each TF had its own electrical signature. More importantly, we show for the first time that addition of cognate double-stranded DNA sequences leads to a specific response: an increase in the conductance of the TF-containing membrane. Strikingly, the effect of cognate DNA was observed when it was added to the trans-side of the membrane (opposite to where the TF was added), strongly suggesting that the TFs span the membrane and that the DNA-binding domain is trans-accessible. Alterations in the primary structure of the TF factors in their basic and DNA-binding regions change the characteristics of the conductance of the protein-containing membranes as well as the response to DNA addition, reinforcing the notion that the changes we measure are due to specific interactions. © 2001 Elsevier Science B.V. 2001 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1510_n1-2_p209_Tosteson http://hdl.handle.net/20.500.12110/paper_00052736_v1510_n1-2_p209_Tosteson |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
DNA binding Lipid bilayer Protein channel Transcription factor double stranded DNA ion channel transcription factor article consensus sequence DNA binding DNA sequence membrane binding membrane conductance priority journal protein lipid interaction Consensus Sequence Dimerization DNA Ion Channels Lipid Bilayers Membrane Potentials Molecular Conformation Protein Binding Transcription Factors |
| spellingShingle |
DNA binding Lipid bilayer Protein channel Transcription factor double stranded DNA ion channel transcription factor article consensus sequence DNA binding DNA sequence membrane binding membrane conductance priority journal protein lipid interaction Consensus Sequence Dimerization DNA Ion Channels Lipid Bilayers Membrane Potentials Molecular Conformation Protein Binding Transcription Factors Ion channels formed by transcription factors recognize consensus DNA sequences |
| topic_facet |
DNA binding Lipid bilayer Protein channel Transcription factor double stranded DNA ion channel transcription factor article consensus sequence DNA binding DNA sequence membrane binding membrane conductance priority journal protein lipid interaction Consensus Sequence Dimerization DNA Ion Channels Lipid Bilayers Membrane Potentials Molecular Conformation Protein Binding Transcription Factors |
| description |
Transcription factors (TFs) are proteins which bind to specific DNA sequences and thus participate in the regulation of the initiation of transcription. We report in this communication our observations that several of these proteins interact with lipid membranes and form ion-permeable channels. For each of the TFs that we studied, the single channel conductance was distinctively different, i.e. each TF had its own electrical signature. More importantly, we show for the first time that addition of cognate double-stranded DNA sequences leads to a specific response: an increase in the conductance of the TF-containing membrane. Strikingly, the effect of cognate DNA was observed when it was added to the trans-side of the membrane (opposite to where the TF was added), strongly suggesting that the TFs span the membrane and that the DNA-binding domain is trans-accessible. Alterations in the primary structure of the TF factors in their basic and DNA-binding regions change the characteristics of the conductance of the protein-containing membranes as well as the response to DNA addition, reinforcing the notion that the changes we measure are due to specific interactions. © 2001 Elsevier Science B.V. |
| title |
Ion channels formed by transcription factors recognize consensus DNA sequences |
| title_short |
Ion channels formed by transcription factors recognize consensus DNA sequences |
| title_full |
Ion channels formed by transcription factors recognize consensus DNA sequences |
| title_fullStr |
Ion channels formed by transcription factors recognize consensus DNA sequences |
| title_full_unstemmed |
Ion channels formed by transcription factors recognize consensus DNA sequences |
| title_sort |
ion channels formed by transcription factors recognize consensus dna sequences |
| publishDate |
2001 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1510_n1-2_p209_Tosteson http://hdl.handle.net/20.500.12110/paper_00052736_v1510_n1-2_p209_Tosteson |
| _version_ |
1768545582442348544 |