Identification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein

Abstract Chloride intracellular channels (CLIC) are non-classical ion channels lacking a signal sequence for membrane targeting. In eukaryotes, they are implicated in cell volume regulation, acidification, and cell cycle. CLICs resemble the omega class of Glutathione S-transferases (GST), yet differ...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Shubha Gururaja Rao, Devasena Ponnalagu, Sowmya Sukur, Harkewal Singh, Shridhar Sanghvi, Yixiao Mei, Ding J. Jin, Harpreet Singh
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3aeea676afc6450284a8be114afbb523
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:3aeea676afc6450284a8be114afbb523
record_format	dspace
spelling	oai:doaj.org-article:3aeea676afc6450284a8be114afbb5232021-12-02T16:08:09ZIdentification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein10.1038/s41598-017-08742-z2045-2322https://doaj.org/article/3aeea676afc6450284a8be114afbb5232017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-08742-zhttps://doaj.org/toc/2045-2322Abstract Chloride intracellular channels (CLIC) are non-classical ion channels lacking a signal sequence for membrane targeting. In eukaryotes, they are implicated in cell volume regulation, acidification, and cell cycle. CLICs resemble the omega class of Glutathione S-transferases (GST), yet differ from them in their ability to form ion channels. They are ubiquitously found in eukaryotes but no prokaryotic homolog has been characterized. We found that indanyloxyacetic acid-94 (IAA-94), a blocker of CLICs, delays the growth of Escherichia coli. In silico analysis showed that the E. coli stringent starvation protein A (SspA) shares sequence and structural homology with CLICs. Similar to CLICs, SspA lacks a signal sequence but contains an omega GST fold. Electrophysiological analysis revealed that SspA auto-inserts into lipid bilayers and forms IAA-94-sensitive ion channels. Substituting the ubiquitously conserved residue leucine 29 to alanine in the pore-forming region increased its single-channel conductance. SspA is essential for cell survival during acid-induced stress, and we found that acidic pH increases the open probability of SspA. Further, IAA-94 delayed the growth of wild-type but not sspA null mutant E. coli. Our results for the first time show that CLIC-like proteins exist in bacteria in the form of SspA, forming functional ion channels.Shubha Gururaja RaoDevasena PonnalaguSowmya SukurHarkewal SinghShridhar SanghviYixiao MeiDing J. JinHarpreet SinghNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Shubha Gururaja Rao Devasena Ponnalagu Sowmya Sukur Harkewal Singh Shridhar Sanghvi Yixiao Mei Ding J. Jin Harpreet Singh Identification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein
description	Abstract Chloride intracellular channels (CLIC) are non-classical ion channels lacking a signal sequence for membrane targeting. In eukaryotes, they are implicated in cell volume regulation, acidification, and cell cycle. CLICs resemble the omega class of Glutathione S-transferases (GST), yet differ from them in their ability to form ion channels. They are ubiquitously found in eukaryotes but no prokaryotic homolog has been characterized. We found that indanyloxyacetic acid-94 (IAA-94), a blocker of CLICs, delays the growth of Escherichia coli. In silico analysis showed that the E. coli stringent starvation protein A (SspA) shares sequence and structural homology with CLICs. Similar to CLICs, SspA lacks a signal sequence but contains an omega GST fold. Electrophysiological analysis revealed that SspA auto-inserts into lipid bilayers and forms IAA-94-sensitive ion channels. Substituting the ubiquitously conserved residue leucine 29 to alanine in the pore-forming region increased its single-channel conductance. SspA is essential for cell survival during acid-induced stress, and we found that acidic pH increases the open probability of SspA. Further, IAA-94 delayed the growth of wild-type but not sspA null mutant E. coli. Our results for the first time show that CLIC-like proteins exist in bacteria in the form of SspA, forming functional ion channels.
format	article
author	Shubha Gururaja Rao Devasena Ponnalagu Sowmya Sukur Harkewal Singh Shridhar Sanghvi Yixiao Mei Ding J. Jin Harpreet Singh
author_facet	Shubha Gururaja Rao Devasena Ponnalagu Sowmya Sukur Harkewal Singh Shridhar Sanghvi Yixiao Mei Ding J. Jin Harpreet Singh
author_sort	Shubha Gururaja Rao
title	Identification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein
title_short	Identification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein
title_full	Identification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein
title_fullStr	Identification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein
title_full_unstemmed	Identification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein
title_sort	identification and characterization of a bacterial homolog of chloride intracellular channel (clic) protein
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/3aeea676afc6450284a8be114afbb523
work_keys_str_mv	AT shubhagururajarao identificationandcharacterizationofabacterialhomologofchlorideintracellularchannelclicprotein AT devasenaponnalagu identificationandcharacterizationofabacterialhomologofchlorideintracellularchannelclicprotein AT sowmyasukur identificationandcharacterizationofabacterialhomologofchlorideintracellularchannelclicprotein AT harkewalsingh identificationandcharacterizationofabacterialhomologofchlorideintracellularchannelclicprotein AT shridharsanghvi identificationandcharacterizationofabacterialhomologofchlorideintracellularchannelclicprotein AT yixiaomei identificationandcharacterizationofabacterialhomologofchlorideintracellularchannelclicprotein AT dingjjin identificationandcharacterizationofabacterialhomologofchlorideintracellularchannelclicprotein AT harpreetsingh identificationandcharacterizationofabacterialhomologofchlorideintracellularchannelclicprotein
_version_	1718384588388040704

Identification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein

Ejemplares similares