Recombinant SEC14-like proteins (TAP) possess GTPase activity

Daniel Habermehl, Petra Kempna, Angelo Azzi, Jean Marc Zingg

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

The three human SEC14-like proteins TAP1, TAP2, and TAP3 were expressed in Escherichia coli and purified by means of an amino-terminal His-tag. The recombinant TAP proteins bound α-, β-, γ-, and δ-tocopherol, certain phospholipids, and squalene. Intriguingly, the TAP proteins showed considerable GTPase activity that was comparable to that of small GTP-binding proteins of the Rab family. Although the TAP proteins contain important motifs to provide GTPase activity, the surrounding secondary structure markedly differed from common G-protein domains. However, these motifs are located in close proximity in the TAP structure and may therefore form an active site for GTP-binding and hydrolysis.

Original languageEnglish (US)
Pages (from-to)254-259
Number of pages6
JournalBiochemical and biophysical research communications
Volume326
Issue number1
DOIs
StatePublished - Dec 31 2004
Externally publishedYes

Keywords

  • CRAL-TRIO
  • GTPase
  • Phospholipids
  • SEC14p
  • Tocopherol
  • Vitamin E

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Recombinant SEC14-like proteins (TAP) possess GTPase activity'. Together they form a unique fingerprint.

Cite this