TOC159 Antibody

1. these data suggest that the Toc159 receptor is required in the import of stearoyl-ACP desaturase and MGD1 synthase into the chloroplasts. PMID: 24184455
2. the contribution of the import receptor Toc159 to the assembly of the chloroplast proteome PMID: 22128122
3. The Toc159 A-domain participates in preprotein selectivity, has typical features of intrinsically unfolded proteins, is highly phosphorylated and possibly released from the rest of the protein by a proteolytic event. PMID: 21057194
4. This review discusses TOC33 and TOC159, the major protein components of the translocon at the outer envelope membrane of chloroplasts (TOC) complex. PMID: 21568939
5. Study show that the overexpression of Toc90 partially complements the albino knockout of Toc159 and restores photoautotrophic growth. PMID: 21220583
6. The A-domain is not simply degraded but it accumulates as a soluble, phosphorylated protein separated from Toc159. PMID: 20457805
7. The A-domains of the Toc159 family members are major determinants of distinct pathways for protein import into plastids. PMID: 20562235
8. Identification of the A-domains will be important for determining their precise function(s), and suggests a role in protein-protein interactions, which may explain how these proteins serve as receptors for such a wide variety of preprotein substrates. PMID: 20042108
9. Embryo development in the atToc132/159 mutants proceeded slowly and was arrested at the transition to the heart stage. PMID: 16435266
10. By combining these models with the measured enzymatic properties of the Toc GTPases, we provide new insights of how the chloroplast protein import cycle may be regulated PMID: 17261588
11. analysis of Toc159- and Toc75-independent import of a transit sequence-less precursor into the inner envelope of chloroplasts PMID: 17636260
12. the three domains commonly referred to as A, G, and M originate from the GTPase G domain, tandemly repeated, and probably evolving toward an unstructured conformation in the case of the A domain. PMID: 17950698
13. Phosphorylation disturbs the association of Toc34, but not of Toc159 with the translocation pore proteins. PMID: 18487635
14. analysis of Arabidopsis Toc33, Toc34, and Toc159-GTPase homodimers PMID: 18541539
15. Data favor a model in which the atToc159 receptor acts as part of a GTP-regulated switch for preprotein recognition at the TOC translocon. PMID: 18824565
16. Toc33 and Toc159 form heterodimer in vivo. PMID: 19010773
17. GTP hydrolysis at atToc159 is not strictly required for preprotein translocation. PMID: 19188370
18. In this study, multiple hybrid mutants were genereated using the Rubisco small subunit transit peptide (TP) and the E1alpha-subunit of pyruvate dehydrogenase TP as representatives mediating import through the Toc159-dependent and -independent pathways. PMID: 19571307
19. Toc33-R130A mutation reduces homodimerization and affects the interaction of Toc33 with Toc159 during protein import into chloroplasts. PMID: 19744928

Show More

Hide All

KEGG: ath:AT4G02510

STRING: 3702.AT4G02510.1

UniGene: At.24962