Bacterial peptidoglycan binds to tubulin

Roman Dziarski, Mark M. Rasenick, Dipika Gupta

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

A search for cellular binding proteins for peptidoglycan (PGN), a CD14- and TLR2-dependent macrophage activator from Gram-positive bacteria, using PGN-affinity chromatography and N-terminal micro-sequencing, revealed that tubulin was a major PGN-binding protein in mouse macrophages. Tubulin also co-eluted with PGN from anti-PGN vancomycin affinity column and bound to PGN coupled to agarose. Tubulin-PGN binding was preferential under the conditions that promote tubulin polymerization, required macromolecular PGN, was competitively inhibited by soluble PGN and tubulin, did not require microtubule-associated proteins, and had an affinity of 100-150 nM. By contrast, binding of tubulin to lipopolysaccharide (LPS) had 2-3 times lower affinity, faster kinetics of binding, and showed positive cooperativity. PGN enhanced tubulin polymerization in the presence of 4 M glycerol, but in the absence of glycerol, both PGN and LPS decreased microtubule polymerization. These results indicate that tubulin is a major PGN-binding protein and that PGN modulates tubulin polymerization. Copyright (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)17-26
Number of pages10
JournalBiochimica et Biophysica Acta - General Subjects
Volume1524
Issue number1
DOIs
StatePublished - Nov 15 2000

Keywords

  • Lipopolysaccharide
  • Microtubule
  • Peptidoglycan
  • Tubulin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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