Chemoreceptors with C-terminal pentapeptides for CheR and CheB binding are abundant in bacteria that maintain host interactions
Chemosensory pathways represent a major prokaryotic signal transduction mechanism that is based on signal sensing by chemoreceptors. An essential feature of chemosensory pathways is the CheR and CheB mediated control of chemoreceptor methylation causing pathway adaptation. At their C-terminal extens...
Main Authors: | , |
---|---|
格式: | Article |
語言: | English |
出版: |
Elsevier
2020-01-01
|
叢編: | Computational and Structural Biotechnology Journal |
主題: | |
在線閱讀: | http://www.sciencedirect.com/science/article/pii/S200103702030338X |
_version_ | 1831579000293556224 |
---|---|
author | Álvaro Ortega Tino Krell |
author_facet | Álvaro Ortega Tino Krell |
author_sort | Álvaro Ortega |
collection | DOAJ |
description | Chemosensory pathways represent a major prokaryotic signal transduction mechanism that is based on signal sensing by chemoreceptors. An essential feature of chemosensory pathways is the CheR and CheB mediated control of chemoreceptor methylation causing pathway adaptation. At their C-terminal extension the Tar and Tsr model chemoreceptors contain a pentapeptide that acts as an additional CheR and CheB binding site. The relevance of this pentapeptide is poorly understood since pentapeptide removal from Tar/Tsr causes receptor inactivation, whereas many other chemoreceptors do not require this pentapeptide for correct function. We report here a bioinformatic analysis of pentapeptide containing chemoreceptors. These receptors were detected in 11 bacterial phyla and represent approximately 10% of all chemoreceptors. Pentapeptide containing chemoreceptors are mainly found in Gram-negative bacteria, are of low abundance in Gram-positive species and almost absent from archaea. Almost 50% of TarH (Tar homologue) ligand binding domain containing chemoreceptors possess pentapeptides, whereas chemoreceptor families with other ligand binding domains are devoid of pentapeptides. The abundance of chemoreceptors with C-terminal pentapeptides correlated negatively with the number of chemoreceptor genes per genome. The consensus sequence reveals a negative net charge for many pentapeptides. Pentapeptide containing chemoreceptors are very abundant in the order Enterobacterales, particularly in the families Pectobacterium and Dickeya, where they represent about 50% of the total number. In contrast, bacteria with primarily free living lifestyles have a reduced number of pentapeptides, such as approximately 1% for Pseudomonadales. It is proposed that pentapeptide function is related to mechanisms that permit host interaction. |
first_indexed | 2024-12-17T16:21:35Z |
format | Article |
id | doaj.art-7eb2c1d90bdd4b6ea3d94fa21c36f57e |
institution | Directory Open Access Journal |
issn | 2001-0370 |
language | English |
last_indexed | 2024-12-17T16:21:35Z |
publishDate | 2020-01-01 |
publisher | Elsevier |
record_format | Article |
series | Computational and Structural Biotechnology Journal |
spelling | doaj.art-7eb2c1d90bdd4b6ea3d94fa21c36f57e2022-12-21T21:41:32ZengElsevierComputational and Structural Biotechnology Journal2001-03702020-01-011819471955Chemoreceptors with C-terminal pentapeptides for CheR and CheB binding are abundant in bacteria that maintain host interactionsÁlvaro Ortega0Tino Krell1Department of Biochemistry and Molecular Biology ‘B’ and Immunology, Faculty of Chemistry, University of Murcia, Regional Campus of International Excellence “Campus Mare Nostrum”, Murcia, SpainDepartment of Environmental Protection, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas, Granada, Spain; Corresponding author at: Estación Experimental del Zaidín, Prof. Albareda 1, Granada 18008, Spain.Chemosensory pathways represent a major prokaryotic signal transduction mechanism that is based on signal sensing by chemoreceptors. An essential feature of chemosensory pathways is the CheR and CheB mediated control of chemoreceptor methylation causing pathway adaptation. At their C-terminal extension the Tar and Tsr model chemoreceptors contain a pentapeptide that acts as an additional CheR and CheB binding site. The relevance of this pentapeptide is poorly understood since pentapeptide removal from Tar/Tsr causes receptor inactivation, whereas many other chemoreceptors do not require this pentapeptide for correct function. We report here a bioinformatic analysis of pentapeptide containing chemoreceptors. These receptors were detected in 11 bacterial phyla and represent approximately 10% of all chemoreceptors. Pentapeptide containing chemoreceptors are mainly found in Gram-negative bacteria, are of low abundance in Gram-positive species and almost absent from archaea. Almost 50% of TarH (Tar homologue) ligand binding domain containing chemoreceptors possess pentapeptides, whereas chemoreceptor families with other ligand binding domains are devoid of pentapeptides. The abundance of chemoreceptors with C-terminal pentapeptides correlated negatively with the number of chemoreceptor genes per genome. The consensus sequence reveals a negative net charge for many pentapeptides. Pentapeptide containing chemoreceptors are very abundant in the order Enterobacterales, particularly in the families Pectobacterium and Dickeya, where they represent about 50% of the total number. In contrast, bacteria with primarily free living lifestyles have a reduced number of pentapeptides, such as approximately 1% for Pseudomonadales. It is proposed that pentapeptide function is related to mechanisms that permit host interaction.http://www.sciencedirect.com/science/article/pii/S200103702030338XChemotaxisChemoreceptorCheRChemosensory pathwayC-terminal pentapeptide |
spellingShingle | Álvaro Ortega Tino Krell Chemoreceptors with C-terminal pentapeptides for CheR and CheB binding are abundant in bacteria that maintain host interactions Computational and Structural Biotechnology Journal Chemotaxis Chemoreceptor CheR Chemosensory pathway C-terminal pentapeptide |
title | Chemoreceptors with C-terminal pentapeptides for CheR and CheB binding are abundant in bacteria that maintain host interactions |
title_full | Chemoreceptors with C-terminal pentapeptides for CheR and CheB binding are abundant in bacteria that maintain host interactions |
title_fullStr | Chemoreceptors with C-terminal pentapeptides for CheR and CheB binding are abundant in bacteria that maintain host interactions |
title_full_unstemmed | Chemoreceptors with C-terminal pentapeptides for CheR and CheB binding are abundant in bacteria that maintain host interactions |
title_short | Chemoreceptors with C-terminal pentapeptides for CheR and CheB binding are abundant in bacteria that maintain host interactions |
title_sort | chemoreceptors with c terminal pentapeptides for cher and cheb binding are abundant in bacteria that maintain host interactions |
topic | Chemotaxis Chemoreceptor CheR Chemosensory pathway C-terminal pentapeptide |
url | http://www.sciencedirect.com/science/article/pii/S200103702030338X |
work_keys_str_mv | AT alvaroortega chemoreceptorswithcterminalpentapeptidesforcherandchebbindingareabundantinbacteriathatmaintainhostinteractions AT tinokrell chemoreceptorswithcterminalpentapeptidesforcherandchebbindingareabundantinbacteriathatmaintainhostinteractions |