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Structural basis for recognition of transcriptional terminator structures by ProQ/FinO domain RNA chaperones

The ProQ/FinO family of RNA binding proteins mediate sRNA-directed gene regulation throughout gram-negative bacteria. Here, we investigate the structural basis for RNA recognition by ProQ/FinO proteins, through the crystal structure of the ProQ/FinO domain of the Legionella pneumophila DNA uptake re...

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Autores principales: Kim, Hyeong Jin, Black, Mazzen, Edwards, Ross A., Peillard-Fiorente, Flora, Panigrahi, Rashmi, Klingler, David, Eidelpes, Reiner, Zeindl, Ricarda, Peng, Shiyun, Su, Jikun, Omar, Ayat R., MacMillan, Andrew M., Kreutz, Christoph, Tollinger, Martin, Charpentier, Xavier, Attaiech, Laetitia, Glover, J. N. Mark
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9674577/
https://www.ncbi.nlm.nih.gov/pubmed/36400772
http://dx.doi.org/10.1038/s41467-022-34875-5
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author Kim, Hyeong Jin
Black, Mazzen
Edwards, Ross A.
Peillard-Fiorente, Flora
Panigrahi, Rashmi
Klingler, David
Eidelpes, Reiner
Zeindl, Ricarda
Peng, Shiyun
Su, Jikun
Omar, Ayat R.
MacMillan, Andrew M.
Kreutz, Christoph
Tollinger, Martin
Charpentier, Xavier
Attaiech, Laetitia
Glover, J. N. Mark
author_facet Kim, Hyeong Jin
Black, Mazzen
Edwards, Ross A.
Peillard-Fiorente, Flora
Panigrahi, Rashmi
Klingler, David
Eidelpes, Reiner
Zeindl, Ricarda
Peng, Shiyun
Su, Jikun
Omar, Ayat R.
MacMillan, Andrew M.
Kreutz, Christoph
Tollinger, Martin
Charpentier, Xavier
Attaiech, Laetitia
Glover, J. N. Mark
author_sort Kim, Hyeong Jin
collection PubMed
description The ProQ/FinO family of RNA binding proteins mediate sRNA-directed gene regulation throughout gram-negative bacteria. Here, we investigate the structural basis for RNA recognition by ProQ/FinO proteins, through the crystal structure of the ProQ/FinO domain of the Legionella pneumophila DNA uptake regulator, RocC, bound to the transcriptional terminator of its primary partner, the sRNA RocR. The structure reveals specific recognition of the 3’ nucleotide of the terminator by a conserved pocket involving a β-turn-α-helix motif, while the hairpin portion of the terminator is recognized by a conserved α-helical N-cap motif. Structure-guided mutagenesis reveals key RNA contact residues that are critical for RocC/RocR to repress the uptake of environmental DNA in L. pneumophila. Structural analysis and RNA binding studies reveal that other ProQ/FinO domains also recognize related transcriptional terminators with different specificities for the length of the 3’ ssRNA tail.
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spelling pubmed-96745772022-11-20 Structural basis for recognition of transcriptional terminator structures by ProQ/FinO domain RNA chaperones Kim, Hyeong Jin Black, Mazzen Edwards, Ross A. Peillard-Fiorente, Flora Panigrahi, Rashmi Klingler, David Eidelpes, Reiner Zeindl, Ricarda Peng, Shiyun Su, Jikun Omar, Ayat R. MacMillan, Andrew M. Kreutz, Christoph Tollinger, Martin Charpentier, Xavier Attaiech, Laetitia Glover, J. N. Mark Nat Commun Article The ProQ/FinO family of RNA binding proteins mediate sRNA-directed gene regulation throughout gram-negative bacteria. Here, we investigate the structural basis for RNA recognition by ProQ/FinO proteins, through the crystal structure of the ProQ/FinO domain of the Legionella pneumophila DNA uptake regulator, RocC, bound to the transcriptional terminator of its primary partner, the sRNA RocR. The structure reveals specific recognition of the 3’ nucleotide of the terminator by a conserved pocket involving a β-turn-α-helix motif, while the hairpin portion of the terminator is recognized by a conserved α-helical N-cap motif. Structure-guided mutagenesis reveals key RNA contact residues that are critical for RocC/RocR to repress the uptake of environmental DNA in L. pneumophila. Structural analysis and RNA binding studies reveal that other ProQ/FinO domains also recognize related transcriptional terminators with different specificities for the length of the 3’ ssRNA tail. Nature Publishing Group UK 2022-11-18 /pmc/articles/PMC9674577/ /pubmed/36400772 http://dx.doi.org/10.1038/s41467-022-34875-5 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Kim, Hyeong Jin
Black, Mazzen
Edwards, Ross A.
Peillard-Fiorente, Flora
Panigrahi, Rashmi
Klingler, David
Eidelpes, Reiner
Zeindl, Ricarda
Peng, Shiyun
Su, Jikun
Omar, Ayat R.
MacMillan, Andrew M.
Kreutz, Christoph
Tollinger, Martin
Charpentier, Xavier
Attaiech, Laetitia
Glover, J. N. Mark
Structural basis for recognition of transcriptional terminator structures by ProQ/FinO domain RNA chaperones
title Structural basis for recognition of transcriptional terminator structures by ProQ/FinO domain RNA chaperones
title_full Structural basis for recognition of transcriptional terminator structures by ProQ/FinO domain RNA chaperones
title_fullStr Structural basis for recognition of transcriptional terminator structures by ProQ/FinO domain RNA chaperones
title_full_unstemmed Structural basis for recognition of transcriptional terminator structures by ProQ/FinO domain RNA chaperones
title_short Structural basis for recognition of transcriptional terminator structures by ProQ/FinO domain RNA chaperones
title_sort structural basis for recognition of transcriptional terminator structures by proq/fino domain rna chaperones
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9674577/
https://www.ncbi.nlm.nih.gov/pubmed/36400772
http://dx.doi.org/10.1038/s41467-022-34875-5
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