Effects of reductive methylation on microtubule assembly. Evidence for an essential amino group in the alpha-chain.

J. Szasz, Robert Burns, H. Sternlicht

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Microtubule protein from bovine brain was reacted at pH 6.7 with formaldehyde and NaCNBH3. These reagents react specifically with protein amino groups, causing their conversion to mono- and dimethylated forms (Jentoft, N., and Dearborn, D. (1979) J. Biol. Chem. 254, 4359-4365). Reductive methylation both inhibited microtubule assembly and induced extensive depolymerization in assembled microtubules. These effects occurred at low levels of methylation (10%) and appeared to arise from an alteration in tubulin which rendered tubulin assembly incompetent. This alteration had no significant effect on colchicine or GTP binding or on the critical tubulin concentration required for assembly. Comparative methylation studies over a range of formaldehyde concentrations involving microtubule polymer, microtubule protein, and several test proteins suggested that assembly inhibition results from the methylation of one or two highly reactive amino groups in the alpha-chain. The reactivities of these amino group(s) were reduced in the polymerized and denatured states.

Original languageEnglish (US)
Pages (from-to)3697-3704
Number of pages8
JournalJournal of Biological Chemistry
Volume257
Issue number7
StatePublished - Apr 10 1982
Externally publishedYes

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Methylation
Microtubules
Tubulin
Microtubule Proteins
Formaldehyde
Depolymerization
Colchicine
Guanosine Triphosphate
Brain
Polymers
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Effects of reductive methylation on microtubule assembly. Evidence for an essential amino group in the alpha-chain. / Szasz, J.; Burns, Robert; Sternlicht, H.

In: Journal of Biological Chemistry, Vol. 257, No. 7, 10.04.1982, p. 3697-3704.

Research output: Contribution to journalArticle

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