Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery

In Escherichia coli, chemoreceptor clustering at a cell pole seems critical for signal amplification and adaptation. However, little is known about the mechanism of localization itself. Here we examined whether the aspartate chemoreceptor (Tar) is inserted directly into the polar membrane by using i...

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Main Authors:	Shiomi, Daisuke, Yoshimoto, Masayuki, Homma, Michio, Kawagishi, Ikuro
Format:	Online
Language:	English
Published:	Blackwell Publishing Ltd 2006
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1513513/

id	pubmed-1513513
recordtype	oai_dc
spelling	pubmed-15135132006-07-24 Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery Shiomi, Daisuke Yoshimoto, Masayuki Homma, Michio Kawagishi, Ikuro Research Articles In Escherichia coli, chemoreceptor clustering at a cell pole seems critical for signal amplification and adaptation. However, little is known about the mechanism of localization itself. Here we examined whether the aspartate chemoreceptor (Tar) is inserted directly into the polar membrane by using its fusion to green fluorescent protein (GFP). After induction of Tar–GFP, fluorescent spots first appeared in lateral membrane regions, and later cell poles became predominantly fluorescent. Unexpectedly, Tar–GFP showed a helical arrangement in lateral regions, which was more apparent when a Tar–GFP derivative with two cysteine residues in the periplasmic domain was cross-linked to form higher oligomers. Moreover, similar distribution was observed even when the cytoplasmic domain of the double cysteine Tar–GFP mutant was replaced by that of the kinase EnvZ, which does not localize to a pole. Observation of GFP–SecE and a translocation-defective MalE–GFP mutant, as well as indirect immunofluorescence microscopy on SecG, suggested that the general protein translocation machinery (Sec) itself is arranged into a helical array, with which Tar is transiently associated. The Sec coil appeared distinct from the MreB coil, an actin-like cytoskeleton. These findings will shed new light on the mechanisms underlying spatial organization of membrane proteins in E. coli. Blackwell Publishing Ltd 2006-05 2006-04-21 /pmc/articles/PMC1513513/ /pubmed/16677301 http://dx.doi.org/10.1111/j.1365-2958.2006.05145.x Text en © 2006 The Authors; Journal compilation © 2006 Blackwell Publishing Ltd
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Shiomi, Daisuke Yoshimoto, Masayuki Homma, Michio Kawagishi, Ikuro
spellingShingle	Shiomi, Daisuke Yoshimoto, Masayuki Homma, Michio Kawagishi, Ikuro Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery
author_facet	Shiomi, Daisuke Yoshimoto, Masayuki Homma, Michio Kawagishi, Ikuro
author_sort	Shiomi, Daisuke
title	Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery
title_short	Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery
title_full	Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery
title_fullStr	Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery
title_full_unstemmed	Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery
title_sort	helical distribution of the bacterial chemoreceptor via colocalization with the sec protein translocation machinery
description	In Escherichia coli, chemoreceptor clustering at a cell pole seems critical for signal amplification and adaptation. However, little is known about the mechanism of localization itself. Here we examined whether the aspartate chemoreceptor (Tar) is inserted directly into the polar membrane by using its fusion to green fluorescent protein (GFP). After induction of Tar–GFP, fluorescent spots first appeared in lateral membrane regions, and later cell poles became predominantly fluorescent. Unexpectedly, Tar–GFP showed a helical arrangement in lateral regions, which was more apparent when a Tar–GFP derivative with two cysteine residues in the periplasmic domain was cross-linked to form higher oligomers. Moreover, similar distribution was observed even when the cytoplasmic domain of the double cysteine Tar–GFP mutant was replaced by that of the kinase EnvZ, which does not localize to a pole. Observation of GFP–SecE and a translocation-defective MalE–GFP mutant, as well as indirect immunofluorescence microscopy on SecG, suggested that the general protein translocation machinery (Sec) itself is arranged into a helical array, with which Tar is transiently associated. The Sec coil appeared distinct from the MreB coil, an actin-like cytoskeleton. These findings will shed new light on the mechanisms underlying spatial organization of membrane proteins in E. coli.
publisher	Blackwell Publishing Ltd
publishDate	2006
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1513513/
_version_	1611384791275405312

Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery

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