Genes encoding Cher-TPR fusion proteins are predominantly found in gene clusters encoding chemosensory pathways with alternative cellular functions.

Chemosensory pathways correspond to major signal transduction mechanisms and can be classified into the functional families flagellum-mediated taxis, type four pili-mediated taxis or pathways with alternative cellular functions (ACF). CheR methyltransferases are core enzymes in all of these families...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Francisco Muñoz-Martínez, Cristina García-Fontana, Miriam Rico-Jiménez, Carlos Alfonso, Tino Krell
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5205a7dd754c4af3970d00ebb485e2dc
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:5205a7dd754c4af3970d00ebb485e2dc
record_format	dspace
spelling	oai:doaj.org-article:5205a7dd754c4af3970d00ebb485e2dc2021-11-18T07:04:41ZGenes encoding Cher-TPR fusion proteins are predominantly found in gene clusters encoding chemosensory pathways with alternative cellular functions.1932-620310.1371/journal.pone.0045810https://doaj.org/article/5205a7dd754c4af3970d00ebb485e2dc2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23029255/?tool=EBIhttps://doaj.org/toc/1932-6203Chemosensory pathways correspond to major signal transduction mechanisms and can be classified into the functional families flagellum-mediated taxis, type four pili-mediated taxis or pathways with alternative cellular functions (ACF). CheR methyltransferases are core enzymes in all of these families. CheR proteins fused to tetratricopeptide repeat (TPR) domains have been reported and we present an analysis of this uncharacterized family. We show that CheR-TPRs are widely distributed in GRAM-negative but almost absent from GRAM-positive bacteria. Most strains contain a single CheR-TPR and its abundance does not correlate with the number of chemoreceptors. The TPR domain fused to CheR is comparatively short and frequently composed of 2 repeats. The majority of CheR-TPR genes were found in gene clusters that harbor multidomain response regulators in which the REC domain is fused to different output domains like HK, GGDEF, EAL, HPT, AAA, PAS, GAF, additional REC, HTH, phosphatase or combinations thereof. The response regulator architectures coincide with those reported for the ACF family of pathways. Since the presence of multidomain response regulators is a distinctive feature of this pathway family, we conclude that CheR-TPR proteins form part of ACF type pathways. The diversity of response regulator output domains suggests that the ACF pathways form a superfamily which regroups many different regulatory mechanisms, in which all CheR-TPR proteins appear to participate. In the second part we characterize WspC of Pseudomonas putida, a representative example of CheR-TPR. The affinities of WspC-Pp for S-adenosylmethionine and S-adenosylhomocysteine were comparable to those of prototypal CheR, indicating that WspC-Pp activity is in analogy to prototypal CheRs controlled by product feed-back inhibition. The removal of the TPR domain did not impact significantly on the binding constants and consequently not on the product feed-back inhibition. WspC-Pp was found to be monomeric, which rules out a role of the TPR domain in self-association.Francisco Muñoz-MartínezCristina García-FontanaMiriam Rico-JiménezCarlos AlfonsoTino KrellPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 9, p e45810 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Francisco Muñoz-Martínez Cristina García-Fontana Miriam Rico-Jiménez Carlos Alfonso Tino Krell Genes encoding Cher-TPR fusion proteins are predominantly found in gene clusters encoding chemosensory pathways with alternative cellular functions.
description	Chemosensory pathways correspond to major signal transduction mechanisms and can be classified into the functional families flagellum-mediated taxis, type four pili-mediated taxis or pathways with alternative cellular functions (ACF). CheR methyltransferases are core enzymes in all of these families. CheR proteins fused to tetratricopeptide repeat (TPR) domains have been reported and we present an analysis of this uncharacterized family. We show that CheR-TPRs are widely distributed in GRAM-negative but almost absent from GRAM-positive bacteria. Most strains contain a single CheR-TPR and its abundance does not correlate with the number of chemoreceptors. The TPR domain fused to CheR is comparatively short and frequently composed of 2 repeats. The majority of CheR-TPR genes were found in gene clusters that harbor multidomain response regulators in which the REC domain is fused to different output domains like HK, GGDEF, EAL, HPT, AAA, PAS, GAF, additional REC, HTH, phosphatase or combinations thereof. The response regulator architectures coincide with those reported for the ACF family of pathways. Since the presence of multidomain response regulators is a distinctive feature of this pathway family, we conclude that CheR-TPR proteins form part of ACF type pathways. The diversity of response regulator output domains suggests that the ACF pathways form a superfamily which regroups many different regulatory mechanisms, in which all CheR-TPR proteins appear to participate. In the second part we characterize WspC of Pseudomonas putida, a representative example of CheR-TPR. The affinities of WspC-Pp for S-adenosylmethionine and S-adenosylhomocysteine were comparable to those of prototypal CheR, indicating that WspC-Pp activity is in analogy to prototypal CheRs controlled by product feed-back inhibition. The removal of the TPR domain did not impact significantly on the binding constants and consequently not on the product feed-back inhibition. WspC-Pp was found to be monomeric, which rules out a role of the TPR domain in self-association.
format	article
author	Francisco Muñoz-Martínez Cristina García-Fontana Miriam Rico-Jiménez Carlos Alfonso Tino Krell
author_facet	Francisco Muñoz-Martínez Cristina García-Fontana Miriam Rico-Jiménez Carlos Alfonso Tino Krell
author_sort	Francisco Muñoz-Martínez
title	Genes encoding Cher-TPR fusion proteins are predominantly found in gene clusters encoding chemosensory pathways with alternative cellular functions.
title_short	Genes encoding Cher-TPR fusion proteins are predominantly found in gene clusters encoding chemosensory pathways with alternative cellular functions.
title_full	Genes encoding Cher-TPR fusion proteins are predominantly found in gene clusters encoding chemosensory pathways with alternative cellular functions.
title_fullStr	Genes encoding Cher-TPR fusion proteins are predominantly found in gene clusters encoding chemosensory pathways with alternative cellular functions.
title_full_unstemmed	Genes encoding Cher-TPR fusion proteins are predominantly found in gene clusters encoding chemosensory pathways with alternative cellular functions.
title_sort	genes encoding cher-tpr fusion proteins are predominantly found in gene clusters encoding chemosensory pathways with alternative cellular functions.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/5205a7dd754c4af3970d00ebb485e2dc
work_keys_str_mv	AT franciscomunozmartinez genesencodingchertprfusionproteinsarepredominantlyfoundingeneclustersencodingchemosensorypathwayswithalternativecellularfunctions AT cristinagarciafontana genesencodingchertprfusionproteinsarepredominantlyfoundingeneclustersencodingchemosensorypathwayswithalternativecellularfunctions AT miriamricojimenez genesencodingchertprfusionproteinsarepredominantlyfoundingeneclustersencodingchemosensorypathwayswithalternativecellularfunctions AT carlosalfonso genesencodingchertprfusionproteinsarepredominantlyfoundingeneclustersencodingchemosensorypathwayswithalternativecellularfunctions AT tinokrell genesencodingchertprfusionproteinsarepredominantlyfoundingeneclustersencodingchemosensorypathwayswithalternativecellularfunctions
_version_	1718423976322007040

Genes encoding Cher-TPR fusion proteins are predominantly found in gene clusters encoding chemosensory pathways with alternative cellular functions.

Ejemplares similares