Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator.
Many members of the TetR family control the transcription of genes involved in multidrug resistance and pathogenicity. RolR (ResorcinolRegulator), the recently reported TetR-type regulator for aromatic catabolism from Corynebacterium glutamicum, distinguishes itself by low sequence similarities and...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2011-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3086911?pdf=render |
| _version_ | 1818516711558610944 |
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| author | De-Feng Li Ning Zhang Yan-Jie Hou Yan Huang Yonglin Hu Ying Zhang Shuang-Jiang Liu Da-Cheng Wang |
| author_facet | De-Feng Li Ning Zhang Yan-Jie Hou Yan Huang Yonglin Hu Ying Zhang Shuang-Jiang Liu Da-Cheng Wang |
| author_sort | De-Feng Li |
| collection | DOAJ |
| description | Many members of the TetR family control the transcription of genes involved in multidrug resistance and pathogenicity. RolR (ResorcinolRegulator), the recently reported TetR-type regulator for aromatic catabolism from Corynebacterium glutamicum, distinguishes itself by low sequence similarities and different regulation from the previously known members of the TetR family. Here we report the crystal structures of RolR in its effector-bound (with resorcinol) and aop- forms at 2.5 Å and 3.6 Å, respectively. The structure of resorcinol-RolR complex reveal that the hydrogen-bonded network mediated by the four-residue motif (Asp94- Arg145- Arg148- Asp149) with two water molecules and the hydrophobic interaction via five residues (Phe107, Leu111, Leu114, Leu142, and Phe172) are the key factors for the recognition and binding between the resorcinol and RolR molecules. The center-to-center separation of the recognition helices h3-h3' is decreased upon effector-binding from 34.9 Å to 30.4 Å. This structural change results in that RolR was unsuitable for DNA binding. Those observations are distinct from that in other TetR members. Structure-based mutagenesis on RolR was carried out and the results confirmed the critical roles of the above mentioned residues for effector-binding specificity and affinity. Similar sequence searches and sequence alignments identified 29 RolR homologues from GenBank, and all the above mentioned residues are highly conserved in the homologues. Based on these structural and other functional investigations, it is proposed that RolR may represent a new subfamily of TetR proteins that are invovled in aromatic degradation and sharing common recognition mode as for RolR. |
| first_indexed | 2024-12-11T00:45:52Z |
| format | Article |
| id | doaj.art-9428928740404f60b916fa67abec5505 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-11T00:45:52Z |
| publishDate | 2011-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-9428928740404f60b916fa67abec55052022-12-22T01:26:47ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-0165e1952910.1371/journal.pone.0019529Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator.De-Feng LiNing ZhangYan-Jie HouYan HuangYonglin HuYing ZhangShuang-Jiang LiuDa-Cheng WangMany members of the TetR family control the transcription of genes involved in multidrug resistance and pathogenicity. RolR (ResorcinolRegulator), the recently reported TetR-type regulator for aromatic catabolism from Corynebacterium glutamicum, distinguishes itself by low sequence similarities and different regulation from the previously known members of the TetR family. Here we report the crystal structures of RolR in its effector-bound (with resorcinol) and aop- forms at 2.5 Å and 3.6 Å, respectively. The structure of resorcinol-RolR complex reveal that the hydrogen-bonded network mediated by the four-residue motif (Asp94- Arg145- Arg148- Asp149) with two water molecules and the hydrophobic interaction via five residues (Phe107, Leu111, Leu114, Leu142, and Phe172) are the key factors for the recognition and binding between the resorcinol and RolR molecules. The center-to-center separation of the recognition helices h3-h3' is decreased upon effector-binding from 34.9 Å to 30.4 Å. This structural change results in that RolR was unsuitable for DNA binding. Those observations are distinct from that in other TetR members. Structure-based mutagenesis on RolR was carried out and the results confirmed the critical roles of the above mentioned residues for effector-binding specificity and affinity. Similar sequence searches and sequence alignments identified 29 RolR homologues from GenBank, and all the above mentioned residues are highly conserved in the homologues. Based on these structural and other functional investigations, it is proposed that RolR may represent a new subfamily of TetR proteins that are invovled in aromatic degradation and sharing common recognition mode as for RolR.http://europepmc.org/articles/PMC3086911?pdf=render |
| spellingShingle | De-Feng Li Ning Zhang Yan-Jie Hou Yan Huang Yonglin Hu Ying Zhang Shuang-Jiang Liu Da-Cheng Wang Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator. PLoS ONE |
| title | Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator. |
| title_full | Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator. |
| title_fullStr | Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator. |
| title_full_unstemmed | Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator. |
| title_short | Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator. |
| title_sort | crystal structures of the transcriptional repressor rolr reveals a novel recognition mechanism between inducer and regulator |
| url | http://europepmc.org/articles/PMC3086911?pdf=render |
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