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Thylakoid ΔpH-dependent precursor proteins bind to a cpTatC–Hcf106 complex before Tha4-dependent transport
Results indicate that precursor binding to the cpTatC–Hcf106 complex constitutes the recognition event for this pathway and that subsequent participation by Tha4 leads to translocation.
A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase
It is reported that Tha4 assembles with cpTatC–Hcf106 during the translocation step, which could explain how the ΔpH/Tat system can assemble translocases to accommodate folded proteins of varied size.
Oligomers of Tha4 Organize at the Thylakoid Tat Translocase during Protein Transport*
A trapdoor mechanism for translocation is proposed whereby aligned oligomers of Tha4 amphipathic helices fold into the membrane to allow formfitting passage of precursor proteins.
Component Specificity for the Thylakoidal Sec and Delta Ph–Dependent Protein Transport Pathways
- H. Mori, E. Summer, Xianyue Ma, K. Cline
- Biology, Environmental ScienceThe Journal of cell biology
- 12 July 1999
These studies provide the first biochemical evidence that Tha4 and Hcf106 are specific components of the Delta pH pathway and provide one line of evidence that cpSecY is used specifically by the Sec pathway.
Phosphatidylserine recognition and induction of apoptotic cell clearance by Drosophila engulfment receptor Draper.
Results indicated that phosphatidylserine serves as an eat-me signal in the phagocytic removal of apoptotic cells in Drosophila and that Draper, an engulfment receptor of Dosophila, is a phosphatido-serine-binding receptor for phagcytosis.
Functional interaction of chloroplast SRP/FtsY with the ALB3 translocase in thylakoids
It is shown that complexes containing cpSRP, cpFtsY, and ALB3 can be precipitated using affinity tags oncpSRP or cpFTSY and inhibited LHCP integration suggesting that a complex containing cp SRP, pSrP, and FtsY must form for proper LHCP Integration.
Post-translational protein translocation into thylakoids by the Sec and DeltapH-dependent pathways.
Chloroplast TatC plays a direct role in thylakoid ΔpH‐dependent protein transport
Requirement of a Tha4-conserved Transmembrane Glutamate in Thylakoid Tat Translocase Assembly Revealed by Biochemical Complementation*
Chemical cross-linking assays showed that the mutated Tha4s failed to be recruited to the receptor complex under transport conditions, indicating a role for the transmembrane glutamate in translocase assembly.
Chloroplast TatC plays a direct role in thylakoid (Delta)pH-dependent protein transport.
cpTatC is an integral thylakoid membrane protein as determined by in vitro chloroplast import and immunoblotting and is relevant to mechanistic models for this system.