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In silico structural analysis of quorum sensing genes inVibrio fischeri

Quorum sensing controls the luminescence of Vibrio fischeri through the transcriptional activator LuxR and the specific autoinducer signal produced by luxI. Amino acid sequences of these two genes were analyzed using bioinformatics tools. LuxI consists of 193 amino acids and appears to contain five...

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Autores principales: Zaghlool, Mohammed, Al-Khayyat, Saeed
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Shiraz University 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5019203/
https://www.ncbi.nlm.nih.gov/pubmed/27844003
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author Zaghlool, Mohammed
Al-Khayyat, Saeed
author_facet Zaghlool, Mohammed
Al-Khayyat, Saeed
author_sort Zaghlool, Mohammed
collection PubMed
description Quorum sensing controls the luminescence of Vibrio fischeri through the transcriptional activator LuxR and the specific autoinducer signal produced by luxI. Amino acid sequences of these two genes were analyzed using bioinformatics tools. LuxI consists of 193 amino acids and appears to contain five α-helices and six ß-sheets when analyzed by SSpro8. LuxI belongs to the autoinducer synthetase family and contains an acetyltransferase domain extending from residues 24 to 110 as MOTIF predicted. LuxR, on the other hand, contains 250 amino acids and has ten α-helices and four ß-sheets. MOTIF predicted LuxR to possess functional motifs; the inducer binding site extending from amino acid residues 23 to 147 and the LuxR activator site extending between amino acids 182 and 236. The InterProScan5 server identified a winged helix- turn-helix DNA binding motif.
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spelling pubmed-50192032016-11-14 In silico structural analysis of quorum sensing genes inVibrio fischeri Zaghlool, Mohammed Al-Khayyat, Saeed Mol Biol Res Commun Original Article Quorum sensing controls the luminescence of Vibrio fischeri through the transcriptional activator LuxR and the specific autoinducer signal produced by luxI. Amino acid sequences of these two genes were analyzed using bioinformatics tools. LuxI consists of 193 amino acids and appears to contain five α-helices and six ß-sheets when analyzed by SSpro8. LuxI belongs to the autoinducer synthetase family and contains an acetyltransferase domain extending from residues 24 to 110 as MOTIF predicted. LuxR, on the other hand, contains 250 amino acids and has ten α-helices and four ß-sheets. MOTIF predicted LuxR to possess functional motifs; the inducer binding site extending from amino acid residues 23 to 147 and the LuxR activator site extending between amino acids 182 and 236. The InterProScan5 server identified a winged helix- turn-helix DNA binding motif. Shiraz University 2015-09 /pmc/articles/PMC5019203/ /pubmed/27844003 Text en This is an Open Access article distributed under the terms of the Creative Commons Attribution License, (http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Article
Zaghlool, Mohammed
Al-Khayyat, Saeed
In silico structural analysis of quorum sensing genes inVibrio fischeri
title In silico structural analysis of quorum sensing genes inVibrio fischeri
title_full In silico structural analysis of quorum sensing genes inVibrio fischeri
title_fullStr In silico structural analysis of quorum sensing genes inVibrio fischeri
title_full_unstemmed In silico structural analysis of quorum sensing genes inVibrio fischeri
title_short In silico structural analysis of quorum sensing genes inVibrio fischeri
title_sort in silico structural analysis of quorum sensing genes invibrio fischeri
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5019203/
https://www.ncbi.nlm.nih.gov/pubmed/27844003
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