A novel tau-tubulin kinase from bovine brain

FEBS Lett. 1995 Sep 18;372(1):59-64. doi: 10.1016/0014-5793(95)00955-9.

Abstract

During purification of tau protein kinase I and II from the bovine brain extract, a new tau protein kinase was detected and purified with phosphocellulose, gel filtration, S-Sepharose and AF-Heparin column chromatography. The molecular mass of the enzyme was determined to be 32 kDa by gel filtration and activity staining on SDS-PAGE. The enzyme is a Ser/Thr protein kinase phosphorylating tau, beta-tubulin, MAP2 and alpha-casein. Employing many synthetic peptides, the recognition site of this enzyme appears to be -SR-. The enzyme requires no second messenger and is inhibited with high concentration of heparin, but not by inhibitors of CKI. These results indicate that this enzyme, tau-tubulin kinase is novel and distinct from TPKI, II and CKI, II.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Animals
  • Brain / enzymology*
  • Caseins / metabolism
  • Cattle
  • Chromatography
  • Electrophoresis, Polyacrylamide Gel
  • Heparin / pharmacology
  • Histones / metabolism
  • Kinetics
  • Microtubule-Associated Proteins / metabolism
  • Molecular Sequence Data
  • Molecular Weight
  • Peptides / chemistry
  • Peptides / metabolism
  • Phosphorylation
  • Potassium Chloride / pharmacology
  • Protein-Serine-Threonine Kinases / chemistry
  • Protein-Serine-Threonine Kinases / isolation & purification*
  • Protein-Serine-Threonine Kinases / metabolism*
  • Substrate Specificity
  • Tubulin / metabolism*
  • tau Proteins / metabolism*

Substances

  • Caseins
  • Histones
  • Microtubule-Associated Proteins
  • Peptides
  • Tubulin
  • tau Proteins
  • Potassium Chloride
  • Adenosine Triphosphate
  • Heparin
  • tau-tubulin kinase
  • Protein-Serine-Threonine Kinases