A Bioinformatics Analysis Reveals a Group of MocR Bacterial Transcriptional Regulators Linked to a Family of Genes Coding for Membrane Proteins

The MocR bacterial transcriptional regulators are characterized by an N-terminal domain, 60 residues long on average, possessing the winged-helix-turn-helix (wHTH) architecture responsible for DNA recognition and binding, linked to a large C-terminal domain (350 residues on average) that is homologo...

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Main Authors: Teresa Milano, Sebastiana Angelaccio, Angela Tramonti, Martino Luigi Di Salvo, Roberto Contestabile, Stefano Pascarella
Format: Article
Language:English
Published: Wiley 2016-01-01
Series:Biochemistry Research International
Online Access:http://dx.doi.org/10.1155/2016/4360285
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author Teresa Milano
Sebastiana Angelaccio
Angela Tramonti
Martino Luigi Di Salvo
Roberto Contestabile
Stefano Pascarella
author_facet Teresa Milano
Sebastiana Angelaccio
Angela Tramonti
Martino Luigi Di Salvo
Roberto Contestabile
Stefano Pascarella
author_sort Teresa Milano
collection DOAJ
description The MocR bacterial transcriptional regulators are characterized by an N-terminal domain, 60 residues long on average, possessing the winged-helix-turn-helix (wHTH) architecture responsible for DNA recognition and binding, linked to a large C-terminal domain (350 residues on average) that is homologous to fold type-I pyridoxal 5′-phosphate (PLP) dependent enzymes like aspartate aminotransferase (AAT). These regulators are involved in the expression of genes taking part in several metabolic pathways directly or indirectly connected to PLP chemistry, many of which are still uncharacterized. A bioinformatics analysis is here reported that studied the features of a distinct group of MocR regulators predicted to be functionally linked to a family of homologous genes coding for integral membrane proteins of unknown function. This group occurs mainly in the Actinobacteria and Gammaproteobacteria phyla. An analysis of the multiple sequence alignments of their wHTH and AAT domains suggested the presence of specificity-determining positions (SDPs). Mapping of SDPs onto a homology model of the AAT domain hinted at possible structural/functional roles in effector recognition. Likewise, SDPs in wHTH domain suggested the basis of specificity of Transcription Factor Binding Site recognition. The results reported represent a framework for rational design of experiments and for bioinformatics analysis of other MocR subgroups.
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spelling doaj-art-16b94d8fe55b464c84b4cee7a5b8c25b2025-02-03T06:07:56ZengWileyBiochemistry Research International2090-22472090-22552016-01-01201610.1155/2016/43602854360285A Bioinformatics Analysis Reveals a Group of MocR Bacterial Transcriptional Regulators Linked to a Family of Genes Coding for Membrane ProteinsTeresa Milano0Sebastiana Angelaccio1Angela Tramonti2Martino Luigi Di Salvo3Roberto Contestabile4Stefano Pascarella5Dipartimento di Scienze Biochimiche, Sapienza Università di Roma, 00185 Roma, ItalyDipartimento di Scienze Biochimiche, Sapienza Università di Roma, 00185 Roma, ItalyDipartimento di Scienze Biochimiche, Sapienza Università di Roma, 00185 Roma, ItalyDipartimento di Scienze Biochimiche, Sapienza Università di Roma, 00185 Roma, ItalyDipartimento di Scienze Biochimiche, Sapienza Università di Roma, 00185 Roma, ItalyDipartimento di Scienze Biochimiche, Sapienza Università di Roma, 00185 Roma, ItalyThe MocR bacterial transcriptional regulators are characterized by an N-terminal domain, 60 residues long on average, possessing the winged-helix-turn-helix (wHTH) architecture responsible for DNA recognition and binding, linked to a large C-terminal domain (350 residues on average) that is homologous to fold type-I pyridoxal 5′-phosphate (PLP) dependent enzymes like aspartate aminotransferase (AAT). These regulators are involved in the expression of genes taking part in several metabolic pathways directly or indirectly connected to PLP chemistry, many of which are still uncharacterized. A bioinformatics analysis is here reported that studied the features of a distinct group of MocR regulators predicted to be functionally linked to a family of homologous genes coding for integral membrane proteins of unknown function. This group occurs mainly in the Actinobacteria and Gammaproteobacteria phyla. An analysis of the multiple sequence alignments of their wHTH and AAT domains suggested the presence of specificity-determining positions (SDPs). Mapping of SDPs onto a homology model of the AAT domain hinted at possible structural/functional roles in effector recognition. Likewise, SDPs in wHTH domain suggested the basis of specificity of Transcription Factor Binding Site recognition. The results reported represent a framework for rational design of experiments and for bioinformatics analysis of other MocR subgroups.http://dx.doi.org/10.1155/2016/4360285
spellingShingle Teresa Milano
Sebastiana Angelaccio
Angela Tramonti
Martino Luigi Di Salvo
Roberto Contestabile
Stefano Pascarella
A Bioinformatics Analysis Reveals a Group of MocR Bacterial Transcriptional Regulators Linked to a Family of Genes Coding for Membrane Proteins
Biochemistry Research International
title A Bioinformatics Analysis Reveals a Group of MocR Bacterial Transcriptional Regulators Linked to a Family of Genes Coding for Membrane Proteins
title_full A Bioinformatics Analysis Reveals a Group of MocR Bacterial Transcriptional Regulators Linked to a Family of Genes Coding for Membrane Proteins
title_fullStr A Bioinformatics Analysis Reveals a Group of MocR Bacterial Transcriptional Regulators Linked to a Family of Genes Coding for Membrane Proteins
title_full_unstemmed A Bioinformatics Analysis Reveals a Group of MocR Bacterial Transcriptional Regulators Linked to a Family of Genes Coding for Membrane Proteins
title_short A Bioinformatics Analysis Reveals a Group of MocR Bacterial Transcriptional Regulators Linked to a Family of Genes Coding for Membrane Proteins
title_sort bioinformatics analysis reveals a group of mocr bacterial transcriptional regulators linked to a family of genes coding for membrane proteins
url http://dx.doi.org/10.1155/2016/4360285
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