Association of high molecular weight proteins with microtubules and their role in microtubule assembly in vitro

D. B. Murphy, G. G. Borisy

Research output: Contribution to journalArticle


High molecular weight components (HMW) specifically associated with microtubule protein purified from porcine brain tissue were separated from tubulin by DEAE Sephadex ion exchange chromatography. Analysis by viscometry, sedimentation, and electron microscopy of the unfractionated microtubule protein, separated HMW and tubulin fractions, and reconstituted mixtures showed that HMW promoted formation of ring structures at 5° and tubule polymerization at 37°. The HMW reassociated with tubulin and was identified in thin sections as 18.9 x 5.6 nm projections attached to the microtubules with a longitudinal periodicity of 32.5 nm. These studies: (1) indicate that the HMW fraction stimulates microtubule assembly by facilitating the formation of ring structures which are apparently intermediates in polymerization, and (2) demonstrate that the HMW associates with microtubules as a structural component projecting from the surface of the microtubule wall.

Original languageEnglish (US)
Pages (from-to)2696-2700
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number7
Publication statusPublished - 1975
Externally publishedYes


ASJC Scopus subject areas

  • General
  • Genetics

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