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

A bioinformatics analysis reveals a group of MocR bacterial transcriptional regulators linked to a family of genes coding for membrane proteins / Milano, Teresa; Angelaccio, Sebastiana; Tramonti, Angela; DI SALVO, Martino Luigi; Contestabile, Roberto; Pascarella, Stefano. - In: BIOCHEMISTRY RESEARCH INTERNATIONAL. - ISSN 2090-2247. - STAMPA. - 2016:(2016), pp. ...-.... [10.1155/2016/4360285]

A bioinformatics analysis reveals a group of MocR bacterial transcriptional regulators linked to a family of genes coding for membrane proteins

MILANO, TERESA;ANGELACCIO, Sebastiana;TRAMONTI, Angela;DI SALVO, Martino Luigi;CONTESTABILE, Roberto;PASCARELLA, Stefano
2016

Abstract

The MocR bacterial transcriptional regulators are characterized by an N-terminal domain, 60 residue long on average, possessing the winged-helix-turn-helix architecture (wHTH) responsible for DNA recognition and binding, linked to a large C-terminal domain (350 residue 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 (SDP). 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.
ycze; yczr, duf161; mocr; membrane proteins; pyridoxal 5-phosphate; fold type-i; plp-dependent enzymes; transcription factor binding sites; dna-protein interaction
01 Pubblicazione su rivista::01a Articolo in rivista
A bioinformatics analysis reveals a group of MocR bacterial transcriptional regulators linked to a family of genes coding for membrane proteins / Milano, Teresa; Angelaccio, Sebastiana; Tramonti, Angela; DI SALVO, Martino Luigi; Contestabile, Roberto; Pascarella, Stefano. - In: BIOCHEMISTRY RESEARCH INTERNATIONAL. - ISSN 2090-2247. - STAMPA. - 2016:(2016), pp. ...-.... [10.1155/2016/4360285]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/874429
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