Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex.

We report a crystal structure of Hfq and catalase HPII from Escherichia coli. The post-transcriptional regulator Hfq plays a key role in the survival of bacteria under stress. A small non-coding RNA (sRNA) DsrA is required for translation of the stationary phase sigma factor RpoS, which is the centr...

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Autores principales:	Koji Yonekura, Masahiro Watanabe, Yuko Kageyama, Kunio Hirata, Masaki Yamamoto, Saori Maki-Yonekura
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/bf66df779b034d8180fc49adf7a7e9c8
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spelling	oai:doaj.org-article:bf66df779b034d8180fc49adf7a7e9c82021-11-18T08:48:09ZPost-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex.1932-620310.1371/journal.pone.0078216https://doaj.org/article/bf66df779b034d8180fc49adf7a7e9c82013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24223139/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203We report a crystal structure of Hfq and catalase HPII from Escherichia coli. The post-transcriptional regulator Hfq plays a key role in the survival of bacteria under stress. A small non-coding RNA (sRNA) DsrA is required for translation of the stationary phase sigma factor RpoS, which is the central regulator of the general stress response. Hfq facilitates efficient translation of rpoS mRNA, which encodes RpoS. Hfq helps in the function of other specific proteins involved in RNA processing, indicating its versatility in the cell. However, structural information regarding its interactions with partners is missing. Here we obtained crystals of Hfq and HPII complexes from cell lysates following attempts to overexpress a foreign membrane protein. HPII is one of two catalases in E. coli and its mRNA is transcribed by an RNA polymerase holoenzyme containing RpoS, which in turn is under positive control of small non-coding RNAs and of the RNA chaperone Hfq. This sigma factor is known to have a pronounced effect on the expression of HPII. The crystal structure reveals that a Hfq hexamer binds each subunit of a HPII tetramer. Each subunit of the Hfq hexamer exhibits a unique binding mode with HPII. The hexamer of Hfq interacts via its distal surface. The proximal and distal surfaces are known to specifically bind different sRNAs, and binding of HPII could affect Hfq function. Hfq-HPII complexation has no effect on catalase HPII activity.Koji YonekuraMasahiro WatanabeYuko KageyamaKunio HirataMasaki YamamotoSaori Maki-YonekuraPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 11, p e78216 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Koji Yonekura Masahiro Watanabe Yuko Kageyama Kunio Hirata Masaki Yamamoto Saori Maki-Yonekura Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex.
description	We report a crystal structure of Hfq and catalase HPII from Escherichia coli. The post-transcriptional regulator Hfq plays a key role in the survival of bacteria under stress. A small non-coding RNA (sRNA) DsrA is required for translation of the stationary phase sigma factor RpoS, which is the central regulator of the general stress response. Hfq facilitates efficient translation of rpoS mRNA, which encodes RpoS. Hfq helps in the function of other specific proteins involved in RNA processing, indicating its versatility in the cell. However, structural information regarding its interactions with partners is missing. Here we obtained crystals of Hfq and HPII complexes from cell lysates following attempts to overexpress a foreign membrane protein. HPII is one of two catalases in E. coli and its mRNA is transcribed by an RNA polymerase holoenzyme containing RpoS, which in turn is under positive control of small non-coding RNAs and of the RNA chaperone Hfq. This sigma factor is known to have a pronounced effect on the expression of HPII. The crystal structure reveals that a Hfq hexamer binds each subunit of a HPII tetramer. Each subunit of the Hfq hexamer exhibits a unique binding mode with HPII. The hexamer of Hfq interacts via its distal surface. The proximal and distal surfaces are known to specifically bind different sRNAs, and binding of HPII could affect Hfq function. Hfq-HPII complexation has no effect on catalase HPII activity.
format	article
author	Koji Yonekura Masahiro Watanabe Yuko Kageyama Kunio Hirata Masaki Yamamoto Saori Maki-Yonekura
author_facet	Koji Yonekura Masahiro Watanabe Yuko Kageyama Kunio Hirata Masaki Yamamoto Saori Maki-Yonekura
author_sort	Koji Yonekura
title	Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex.
title_short	Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex.
title_full	Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex.
title_fullStr	Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex.
title_full_unstemmed	Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex.
title_sort	post-transcriptional regulator hfq binds catalase hpii: crystal structure of the complex.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/bf66df779b034d8180fc49adf7a7e9c8
work_keys_str_mv	AT kojiyonekura posttranscriptionalregulatorhfqbindscatalasehpiicrystalstructureofthecomplex AT masahirowatanabe posttranscriptionalregulatorhfqbindscatalasehpiicrystalstructureofthecomplex AT yukokageyama posttranscriptionalregulatorhfqbindscatalasehpiicrystalstructureofthecomplex AT kuniohirata posttranscriptionalregulatorhfqbindscatalasehpiicrystalstructureofthecomplex AT masakiyamamoto posttranscriptionalregulatorhfqbindscatalasehpiicrystalstructureofthecomplex AT saorimakiyonekura posttranscriptionalregulatorhfqbindscatalasehpiicrystalstructureofthecomplex
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Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex.

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