Direct interaction between EFL1 and SBDS is mediated by an intrinsically disordered insertion domain

Nozomi Asano, Haruka Atsuumi, Akiyoshi Nakamura, Yoshikazu Tanaka, Isao Tanaka, Min Yao

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

Removal of anti-association factor, Tif6 (eIF6), by elongation factor-like 1 (EFL1) and Shwachman-Bodian-Diamond syndrome (SBDS) protein is a critical step in the late stage of ribosome maturation. Although EFL1 is known to have GTPase activity that is stimulated by SBDS, how they cooperatively trigger dissociation of Tif6 from the ribosome remains to be elucidated. In the present study, the interaction between EFL1 and SBDS was analyzed by size exclusion chromatography, gel shift assay, and isothermal titration calorimetry (ITC). The results showed that EFL1 interacted directly with SBDS. ITC experiments using domain-truncated mutants showed that the interaction between EFL1 and SBDS is governed by the insertion domain of EFL1 and domains II-III of SBDS. Circular dichroism spectroscopy showed that the insertion domain of EFL1 has a random structure in the absence of SBDS, whereas the disadvantageous entropy change observed on ITC suggested a fixed conformation coupled with complex formation with SBDS. Based on these observations together with those reported previously, we propose roles of EFL1 and SBDS in ribosomal maturation.

Original languageEnglish
Pages (from-to)1251-1256
Number of pages6
JournalBiochemical and biophysical research communications
Volume443
Issue number4
DOIs
Publication statusPublished - 2014 Jan 24
Externally publishedYes

Keywords

  • Circular dichroism
  • Interaction
  • Intrinsically disordered protein
  • Isothermal titration calorimetry
  • Ribosome biogenesis

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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