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pH sensitivity of the GTPase Toc33 as a regulatory circuit for protein translocation into chloroplasts.
- Source :
-
Plant & cell physiology [Plant Cell Physiol] 2008 Dec; Vol. 49 (12), pp. 1917-21. Date of Electronic Publication: 2008 Nov 10. - Publication Year :
- 2008
-
Abstract
- 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.
Details
- Language :
- English
- ISSN :
- 1471-9053
- Volume :
- 49
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Plant & cell physiology
- Publication Type :
- Academic Journal
- Accession number :
- 19001421
- Full Text :
- https://doi.org/10.1093/pcp/pcn171