期刊
FEBS LETTERS
卷 540, 期 1-3, 页码 96-100出版社
WILEY
DOI: 10.1016/S0014-5793(03)00231-X
关键词
cpTat pathway; thylakoid; kinetics; cooperativity
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. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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