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A Minimum of Three Motifs Is Essential for Optimal Binding of Pseudomurein Cell Wall-Binding Domain of Methanothermobacter thermautotrophicus

We have biochemically and functionally characterized the pseudomurein cell wall-binding (PMB) domain that is present at the C-terminus of the Surface (S)-layer protein MTH719 from Methanothermobacter thermautotrophicus. Chemical denaturation of the protein with guanidinium hydrochloride occurred at...

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Detalles Bibliográficos
Autores principales: Visweswaran, Ganesh Ram R., Dijkstra, Bauke W., Kok, Jan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3124540/
https://www.ncbi.nlm.nih.gov/pubmed/21738718
http://dx.doi.org/10.1371/journal.pone.0021582
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author Visweswaran, Ganesh Ram R.
Dijkstra, Bauke W.
Kok, Jan
author_facet Visweswaran, Ganesh Ram R.
Dijkstra, Bauke W.
Kok, Jan
author_sort Visweswaran, Ganesh Ram R.
collection PubMed
description We have biochemically and functionally characterized the pseudomurein cell wall-binding (PMB) domain that is present at the C-terminus of the Surface (S)-layer protein MTH719 from Methanothermobacter thermautotrophicus. Chemical denaturation of the protein with guanidinium hydrochloride occurred at 3.8 M. A PMB-GFP fusion protein not only binds to intact pseudomurein of methanogenic archaea, but also to spheroplasts of lysozyme-treated bacterial cells. This binding is pH dependent. At least two of the three motifs that are present in the domain are necessary for binding. Limited proteolysis revealed a possible cleavage site in the spacing sequence between motifs 1 and 2 of the PMB domain, indicating that the motif region itself is protected from proteases.
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spelling pubmed-31245402011-07-07 A Minimum of Three Motifs Is Essential for Optimal Binding of Pseudomurein Cell Wall-Binding Domain of Methanothermobacter thermautotrophicus Visweswaran, Ganesh Ram R. Dijkstra, Bauke W. Kok, Jan PLoS One Research Article We have biochemically and functionally characterized the pseudomurein cell wall-binding (PMB) domain that is present at the C-terminus of the Surface (S)-layer protein MTH719 from Methanothermobacter thermautotrophicus. Chemical denaturation of the protein with guanidinium hydrochloride occurred at 3.8 M. A PMB-GFP fusion protein not only binds to intact pseudomurein of methanogenic archaea, but also to spheroplasts of lysozyme-treated bacterial cells. This binding is pH dependent. At least two of the three motifs that are present in the domain are necessary for binding. Limited proteolysis revealed a possible cleavage site in the spacing sequence between motifs 1 and 2 of the PMB domain, indicating that the motif region itself is protected from proteases. Public Library of Science 2011-06-27 /pmc/articles/PMC3124540/ /pubmed/21738718 http://dx.doi.org/10.1371/journal.pone.0021582 Text en Visweswaran et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Visweswaran, Ganesh Ram R.
Dijkstra, Bauke W.
Kok, Jan
A Minimum of Three Motifs Is Essential for Optimal Binding of Pseudomurein Cell Wall-Binding Domain of Methanothermobacter thermautotrophicus
title A Minimum of Three Motifs Is Essential for Optimal Binding of Pseudomurein Cell Wall-Binding Domain of Methanothermobacter thermautotrophicus
title_full A Minimum of Three Motifs Is Essential for Optimal Binding of Pseudomurein Cell Wall-Binding Domain of Methanothermobacter thermautotrophicus
title_fullStr A Minimum of Three Motifs Is Essential for Optimal Binding of Pseudomurein Cell Wall-Binding Domain of Methanothermobacter thermautotrophicus
title_full_unstemmed A Minimum of Three Motifs Is Essential for Optimal Binding of Pseudomurein Cell Wall-Binding Domain of Methanothermobacter thermautotrophicus
title_short A Minimum of Three Motifs Is Essential for Optimal Binding of Pseudomurein Cell Wall-Binding Domain of Methanothermobacter thermautotrophicus
title_sort minimum of three motifs is essential for optimal binding of pseudomurein cell wall-binding domain of methanothermobacter thermautotrophicus
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3124540/
https://www.ncbi.nlm.nih.gov/pubmed/21738718
http://dx.doi.org/10.1371/journal.pone.0021582
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