Protein transport via the cpTat pathway displays cooperativity and is stimulated by transport-incompetent substrate.
Kinetic analyses of cpTat-mediated protein transport across the thylakoid membrane were conducted, revealing three important characteristics of this translocation pathway. First, transport via the cpTAT system displays a non-Michaelis-Menten, sigmoidal rate-substrate relationship with an apparent Hill coefficient of 1.80, indicative of positive homotropic cooperativity. Second, the presence of transport-incompetent substrates was found not to competitively inhibit the translocation of transport-competent substrates. However, the presence of low concentrations of transport-incompetent protein enhances the transport of wild type substrate. Together, these findings suggest that interaction between Tat machinery components and both transport-competent and transport-incompetent protein may elicit a cooperative effect on the translocation rate.
Alder
Natahan N
NN
Division of Biological Sciences, Section of Plant Biology, University of California, One Shields Avenue, Davis, CA 95616, USA.
Theg
Steven M
SM
D015696:Gene Products, tat / Q000378:metabolism*; D007700:Kinetics; D021381:Protein Transport; D013379:Substrate Specificity
D015696:Gene Products, tat