Our hosting provider is experiencing network issues which may result in intermittent downtime. We apologize for any inconveniences this may cause.

Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

pH sensitivity of the GTPase Toc33 as a regulatory circuit for protein translocation into chloroplasts.

The properties of membrane-embedded GTPases are investigated to understand translocation of preprotein across the outer envelope of chloroplasts. The homo- and heterodimerization events of the GTPases had been established previously. We show that the hydrolytic activity of the GTPase Toc33 is pH insensitive in the homodimeric conformation but has a bell-shaped pH optimum in the monomeric conformation. Further, Toc33 GTPase homodimerization and protein translocation into chloroplasts are pH sensitive as well. pH sensitivity might serve to regulate translocation; alternatively, the documented pH sensitivity might reflect a mechanistic requirement for GTPase silencing during translocation as the GTPase switches between homo- and heterodimeric conformations.

Pubmed ID: 19001421

Authors

  • Bionda T
  • Koenig P
  • Oreb M
  • Tews I
  • Schleiff E

Journal

Plant & cell physiology

Publication Data

December 8, 2008

Associated Grants

None

Mesh Terms

  • Arabidopsis
  • Arabidopsis Proteins
  • Chloroplasts
  • GTP Phosphohydrolases
  • Hydrogen-Ion Concentration
  • Membrane Proteins
  • Protein Binding
  • Protein Multimerization
  • Protein Precursors
  • Protein Transport