В сучасному динамічно змінюваному світі університет - це перш за все вищий навчальний заклад, який є індикатором цивілізаційності регіону та держави. Проте у наші дні класичні університети постали перед серйозними викликами часу.В современном динамически изменяющемся мире университет - это прежде всего высшее учебное заведение, которое является индикатором цивилизационности региона и государства. Однако в наши дни классические университеты встали перед серьезными вызовами времени

Breukink, E.

de Kruijff, B.

den Blaauwen, T.

Lutters, M.

Martin, N.I.

Mohammadi, T.

Sijbrandi, R.

Verheul, J.

PubMed

Tamimount Mohammadi

Robert Sijbrandi

Mandy Lutters

Jolanda Verheul

Nathaniel I. Martin

Tanneke den Blaauwen

Ben de Kruijff

Eefjan Breukink

Crossref

Journal of Biological Chemistry

Specificity of the Transport of Lipid II by FtsW in Escherichia coli

Synthesis of biogenic membranes requires transbilayer movement of lipid-linked sugar molecules. This biological process, which is fundamental in prokaryotic cells, remains as yet not clearly understood. In order to obtain insights into the molecular basis of its mode of action, we analyzed the structure-function relationship between Lipid II, the important building block of the bacterial cell wall, and its inner membrane-localized transporter FtsW. Here, we show that the predicted transmembrane helix 4 of Escherichia coli FtsW (this protein consists of 10 predicted transmembrane segments) is required for the transport activity of the protein. We have identified two charged residues (Arg(145) and Lys(153)) within this segment that are specifically involved in the flipping of Lipid II. Mutating these two amino acids to uncharged ones affected the transport activity of FtsW. This was consistent with loss of in vivo activity of the mutants, as manifested by their inability to complement a temperature-sensitive strain of FtsW. The transport activity of FtsW could be inhibited with a Lipid II variant having an additional size of 420 Da. Reducing the size of this analog by about 274 Da resulted in the resumption of the transport activity of FtsW. This suggests that the integral membrane protein FtsW forms a size-restricted porelike structure, which accommodates Lipid II during transport across the bacterial cytoplasmic membrane

Mohammadi, Tamimount

Sijbrandi, Robert

Lutters, Mandy

Verheul, Jolanda

Martin, Nathaniel I

den Blaauwen, Tanneke

de Kruijff, Ben

Breukink, Eefjan

Utrecht University Repository

Specificity of the transport of lipid II by FtsW in Escherichia coli

International Migration, Integration and Social Cohesion online publications

NARCIS 

Sub Membrane Biochemistry & Biophysics

Sub Medicinal Chemistry & Chemical biol.

Membrane Biochemistry and Biophysics

Molecular Pharmacy

FWN – Publicaties zonder aanstelling Universiteit Leide

Blaauwen, T. den

Kruijff, B. de

Leiden University Scholary Publications

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