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The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase
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| Zeitschriftentitel: | Journal of Bacteriology |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | Journal of Bacteriology, 184, 2002, 14, S. 3957-3964 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
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| Schlagwörter: |
| author_facet |
Pande, Suchira Makela, Anna Dove, Simon L. Nickels, Bryce E. Hochschild, Ann Hinton, Deborah M. Pande, Suchira Makela, Anna Dove, Simon L. Nickels, Bryce E. Hochschild, Ann Hinton, Deborah M. |
|---|---|
| author |
Pande, Suchira Makela, Anna Dove, Simon L. Nickels, Bryce E. Hochschild, Ann Hinton, Deborah M. |
| spellingShingle |
Pande, Suchira Makela, Anna Dove, Simon L. Nickels, Bryce E. Hochschild, Ann Hinton, Deborah M. Journal of Bacteriology The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase Molecular Biology Microbiology |
| author_sort |
pande, suchira |
| spelling |
Pande, Suchira Makela, Anna Dove, Simon L. Nickels, Bryce E. Hochschild, Ann Hinton, Deborah M. 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.184.14.3957-3964.2002 <jats:title>ABSTRACT</jats:title><jats:p>Transcription from bacteriophage T4 middle promoters uses<jats:italic>Escherichia coli</jats:italic>RNA polymerase together with the T4 transcriptional activator MotA and the T4 coactivator AsiA. AsiA binds tightly within the C-terminal portion of the σ<jats:sup>70</jats:sup>subunit of RNA polymerase, while MotA binds to the 9-bp MotA box motif, which is centered at −30, and also interacts with σ<jats:sup>70</jats:sup>. We show here that the N-terminal half of MotA (MotA<jats:sup>NTD</jats:sup>), which is thought to include the activation domain, interacts with the C-terminal region of σ<jats:sup>70</jats:sup>in an<jats:italic>E. coli</jats:italic>two-hybrid assay. Replacement of the C-terminal 17 residues of σ<jats:sup>70</jats:sup>with comparable σ<jats:sup>38</jats:sup>residues abolishes the interaction with MotA<jats:sup>NTD</jats:sup>in this assay, as does the introduction of the amino acid substitution R608C. Furthermore, in vitro transcription experiments indicate that a polymerase reconstituted with a σ<jats:sup>70</jats:sup>that lacks C-terminal amino acids 604 to 613 or 608 to 613 is defective for MotA-dependent activation. We also show that a proteolyzed fragment of MotA that contains the C-terminal half (MotA<jats:sup>CTD</jats:sup>) binds DNA with a<jats:italic>K</jats:italic><jats:sub>D(app)</jats:sub>that is similar to that of full-length MotA. Our results support a model for MotA-dependent activation in which protein-protein contact between DNA-bound MotA and the far-C-terminal region of σ<jats:sup>70</jats:sup>helps to substitute functionally for an interaction between σ<jats:sup>70</jats:sup>and a promoter −35 element.</jats:p> The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ<sup>70</sup>Subunit of<i>Escherichia coli</i>RNA Polymerase Journal of Bacteriology |
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10.1128/jb.184.14.3957-3964.2002 |
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American Society for Microbiology, 2002 |
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American Society for Microbiology, 2002 |
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0021-9193 1098-5530 |
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0021-9193 1098-5530 |
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2002 |
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American Society for Microbiology |
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Journal of Bacteriology |
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49 |
| title |
The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase |
| title_unstemmed |
The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase |
| title_full |
The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase |
| title_fullStr |
The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase |
| title_full_unstemmed |
The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase |
| title_short |
The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase |
| title_sort |
the bacteriophage t4 transcription activator mota interacts with the far-c-terminal region of the σ<sup>70</sup>subunit of<i>escherichia coli</i>rna polymerase |
| topic |
Molecular Biology Microbiology |
| url |
http://dx.doi.org/10.1128/jb.184.14.3957-3964.2002 |
| publishDate |
2002 |
| physical |
3957-3964 |
| description |
<jats:title>ABSTRACT</jats:title><jats:p>Transcription from bacteriophage T4 middle promoters uses<jats:italic>Escherichia coli</jats:italic>RNA polymerase together with the T4 transcriptional activator MotA and the T4 coactivator AsiA. AsiA binds tightly within the C-terminal portion of the σ<jats:sup>70</jats:sup>subunit of RNA polymerase, while MotA binds to the 9-bp MotA box motif, which is centered at −30, and also interacts with σ<jats:sup>70</jats:sup>. We show here that the N-terminal half of MotA (MotA<jats:sup>NTD</jats:sup>), which is thought to include the activation domain, interacts with the C-terminal region of σ<jats:sup>70</jats:sup>in an<jats:italic>E. coli</jats:italic>two-hybrid assay. Replacement of the C-terminal 17 residues of σ<jats:sup>70</jats:sup>with comparable σ<jats:sup>38</jats:sup>residues abolishes the interaction with MotA<jats:sup>NTD</jats:sup>in this assay, as does the introduction of the amino acid substitution R608C. Furthermore, in vitro transcription experiments indicate that a polymerase reconstituted with a σ<jats:sup>70</jats:sup>that lacks C-terminal amino acids 604 to 613 or 608 to 613 is defective for MotA-dependent activation. We also show that a proteolyzed fragment of MotA that contains the C-terminal half (MotA<jats:sup>CTD</jats:sup>) binds DNA with a<jats:italic>K</jats:italic><jats:sub>D(app)</jats:sub>that is similar to that of full-length MotA. Our results support a model for MotA-dependent activation in which protein-protein contact between DNA-bound MotA and the far-C-terminal region of σ<jats:sup>70</jats:sup>helps to substitute functionally for an interaction between σ<jats:sup>70</jats:sup>and a promoter −35 element.</jats:p> |
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| author | Pande, Suchira, Makela, Anna, Dove, Simon L., Nickels, Bryce E., Hochschild, Ann, Hinton, Deborah M. |
| author_facet | Pande, Suchira, Makela, Anna, Dove, Simon L., Nickels, Bryce E., Hochschild, Ann, Hinton, Deborah M., Pande, Suchira, Makela, Anna, Dove, Simon L., Nickels, Bryce E., Hochschild, Ann, Hinton, Deborah M. |
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| description | <jats:title>ABSTRACT</jats:title><jats:p>Transcription from bacteriophage T4 middle promoters uses<jats:italic>Escherichia coli</jats:italic>RNA polymerase together with the T4 transcriptional activator MotA and the T4 coactivator AsiA. AsiA binds tightly within the C-terminal portion of the σ<jats:sup>70</jats:sup>subunit of RNA polymerase, while MotA binds to the 9-bp MotA box motif, which is centered at −30, and also interacts with σ<jats:sup>70</jats:sup>. We show here that the N-terminal half of MotA (MotA<jats:sup>NTD</jats:sup>), which is thought to include the activation domain, interacts with the C-terminal region of σ<jats:sup>70</jats:sup>in an<jats:italic>E. coli</jats:italic>two-hybrid assay. Replacement of the C-terminal 17 residues of σ<jats:sup>70</jats:sup>with comparable σ<jats:sup>38</jats:sup>residues abolishes the interaction with MotA<jats:sup>NTD</jats:sup>in this assay, as does the introduction of the amino acid substitution R608C. Furthermore, in vitro transcription experiments indicate that a polymerase reconstituted with a σ<jats:sup>70</jats:sup>that lacks C-terminal amino acids 604 to 613 or 608 to 613 is defective for MotA-dependent activation. We also show that a proteolyzed fragment of MotA that contains the C-terminal half (MotA<jats:sup>CTD</jats:sup>) binds DNA with a<jats:italic>K</jats:italic><jats:sub>D(app)</jats:sub>that is similar to that of full-length MotA. Our results support a model for MotA-dependent activation in which protein-protein contact between DNA-bound MotA and the far-C-terminal region of σ<jats:sup>70</jats:sup>helps to substitute functionally for an interaction between σ<jats:sup>70</jats:sup>and a promoter −35 element.</jats:p> |
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| imprint | American Society for Microbiology, 2002 |
| imprint_str_mv | American Society for Microbiology, 2002 |
| institution | DE-15, DE-Rs1, DE-Pl11, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4 |
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| physical | 3957-3964 |
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| spelling | Pande, Suchira Makela, Anna Dove, Simon L. Nickels, Bryce E. Hochschild, Ann Hinton, Deborah M. 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.184.14.3957-3964.2002 <jats:title>ABSTRACT</jats:title><jats:p>Transcription from bacteriophage T4 middle promoters uses<jats:italic>Escherichia coli</jats:italic>RNA polymerase together with the T4 transcriptional activator MotA and the T4 coactivator AsiA. AsiA binds tightly within the C-terminal portion of the σ<jats:sup>70</jats:sup>subunit of RNA polymerase, while MotA binds to the 9-bp MotA box motif, which is centered at −30, and also interacts with σ<jats:sup>70</jats:sup>. We show here that the N-terminal half of MotA (MotA<jats:sup>NTD</jats:sup>), which is thought to include the activation domain, interacts with the C-terminal region of σ<jats:sup>70</jats:sup>in an<jats:italic>E. coli</jats:italic>two-hybrid assay. Replacement of the C-terminal 17 residues of σ<jats:sup>70</jats:sup>with comparable σ<jats:sup>38</jats:sup>residues abolishes the interaction with MotA<jats:sup>NTD</jats:sup>in this assay, as does the introduction of the amino acid substitution R608C. Furthermore, in vitro transcription experiments indicate that a polymerase reconstituted with a σ<jats:sup>70</jats:sup>that lacks C-terminal amino acids 604 to 613 or 608 to 613 is defective for MotA-dependent activation. We also show that a proteolyzed fragment of MotA that contains the C-terminal half (MotA<jats:sup>CTD</jats:sup>) binds DNA with a<jats:italic>K</jats:italic><jats:sub>D(app)</jats:sub>that is similar to that of full-length MotA. Our results support a model for MotA-dependent activation in which protein-protein contact between DNA-bound MotA and the far-C-terminal region of σ<jats:sup>70</jats:sup>helps to substitute functionally for an interaction between σ<jats:sup>70</jats:sup>and a promoter −35 element.</jats:p> The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ<sup>70</sup>Subunit of<i>Escherichia coli</i>RNA Polymerase Journal of Bacteriology |
| spellingShingle | Pande, Suchira, Makela, Anna, Dove, Simon L., Nickels, Bryce E., Hochschild, Ann, Hinton, Deborah M., Journal of Bacteriology, The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase, Molecular Biology, Microbiology |
| title | The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase |
| title_full | The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase |
| title_fullStr | The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase |
| title_full_unstemmed | The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase |
| title_short | The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase |
| title_sort | the bacteriophage t4 transcription activator mota interacts with the far-c-terminal region of the σ<sup>70</sup>subunit of<i>escherichia coli</i>rna polymerase |
| title_unstemmed | The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase |
| topic | Molecular Biology, Microbiology |
| url | http://dx.doi.org/10.1128/jb.184.14.3957-3964.2002 |