Competitive interactions of ligands and macromolecular crowders with maltose binding protein.

Cellular signaling involves a cascade of recognition events occurring in a complex environment with high concentrations of proteins, polysaccharides, and other macromolecules. The influence of macromolecular crowders on protein binding affinity through hard-core repulsion is well studied, and possib...

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Autores principales:	Andrew C Miklos, Matthew Sumpter, Huan-Xiang Zhou
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/587f32e59ae544599438900f5bdcd649
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spelling	oai:doaj.org-article:587f32e59ae544599438900f5bdcd6492021-11-18T08:52:33ZCompetitive interactions of ligands and macromolecular crowders with maltose binding protein.1932-620310.1371/journal.pone.0074969https://doaj.org/article/587f32e59ae544599438900f5bdcd6492013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24124463/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Cellular signaling involves a cascade of recognition events occurring in a complex environment with high concentrations of proteins, polysaccharides, and other macromolecules. The influence of macromolecular crowders on protein binding affinity through hard-core repulsion is well studied, and possible contributions of protein-crowder soft attraction have been implicated recently. Here we present direct evidence for weak association of maltose binding protein (MBP) with a polysaccharide crowder Ficoll, and that this association effectively competes with the binding of the natural ligand, maltose. Titration data over wide ranges of maltose and Ficoll concentrations fit well with a three-state competitive binding model. Broadening of MBP (1)H-(15)N TROSY spectra by the addition of Ficoll indicates weak protein-crowder association, and subsequent recovery of sharp NMR peaks upon addition of maltose indicates that the interactions of the crowder and the ligand with MBP are competitive. We hypothesize that, in the Escherichia coli periplasm, the competitive interactions of polysaccharides and maltose with MBP could allow MBP to shuttle between the peptidoglycan attached to the outer membrane and the ATP-binding cassette transporter in the inner membrane.Andrew C MiklosMatthew SumpterHuan-Xiang ZhouPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 10, p e74969 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Andrew C Miklos Matthew Sumpter Huan-Xiang Zhou Competitive interactions of ligands and macromolecular crowders with maltose binding protein.
description	Cellular signaling involves a cascade of recognition events occurring in a complex environment with high concentrations of proteins, polysaccharides, and other macromolecules. The influence of macromolecular crowders on protein binding affinity through hard-core repulsion is well studied, and possible contributions of protein-crowder soft attraction have been implicated recently. Here we present direct evidence for weak association of maltose binding protein (MBP) with a polysaccharide crowder Ficoll, and that this association effectively competes with the binding of the natural ligand, maltose. Titration data over wide ranges of maltose and Ficoll concentrations fit well with a three-state competitive binding model. Broadening of MBP (1)H-(15)N TROSY spectra by the addition of Ficoll indicates weak protein-crowder association, and subsequent recovery of sharp NMR peaks upon addition of maltose indicates that the interactions of the crowder and the ligand with MBP are competitive. We hypothesize that, in the Escherichia coli periplasm, the competitive interactions of polysaccharides and maltose with MBP could allow MBP to shuttle between the peptidoglycan attached to the outer membrane and the ATP-binding cassette transporter in the inner membrane.
format	article
author	Andrew C Miklos Matthew Sumpter Huan-Xiang Zhou
author_facet	Andrew C Miklos Matthew Sumpter Huan-Xiang Zhou
author_sort	Andrew C Miklos
title	Competitive interactions of ligands and macromolecular crowders with maltose binding protein.
title_short	Competitive interactions of ligands and macromolecular crowders with maltose binding protein.
title_full	Competitive interactions of ligands and macromolecular crowders with maltose binding protein.
title_fullStr	Competitive interactions of ligands and macromolecular crowders with maltose binding protein.
title_full_unstemmed	Competitive interactions of ligands and macromolecular crowders with maltose binding protein.
title_sort	competitive interactions of ligands and macromolecular crowders with maltose binding protein.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/587f32e59ae544599438900f5bdcd649
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Competitive interactions of ligands and macromolecular crowders with maltose binding protein.

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