T. NÃgele - Academia.edu (original) (raw)
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University of Medicine and Pharmacy "Carol Davila" Bucharest
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Papers by T. NÃgele
Journal of Molecular Biology, 2003
Sensory rhodopsin II, a repellent phototaxis receptor from Natronobacterium pharaonis (NpSRII) fo... more Sensory rhodopsin II, a repellent phototaxis receptor from Natronobacterium pharaonis (NpSRII) forms a tight complex with its cognate transducer (NpHtrII). Light excitation of the receptor triggers conformational changes in both proteins, thereby activating the cellular two-component signalling cascade. In membranes, the two proteins form a 2:2 complex, which dissociates to a 1:1 heterodimer in micelles. Complexed to the transducer sensory rhodopsin II is no longer capable of light-driven proton pumping. In order to elucidate the dimerisation and the size of the receptor-binding domain of the transducer, isothermal titration calorimetry and electrophysiological experiments have been carried out. It is shown, that an N-terminal sequence of 114 amino acid residues is sufficient for tight binding (K d ¼ 240 nM; DH ¼ 217:6 kJ mol 21 ) and for inhibiting the proton transfer. These data and results obtained from selected sitedirected mutants indicate a synergistic interplay of transducer transmembrane domain (1 -82) and cytoplasmic peptide (83 -114) leading to an optimal and specific interaction between receptor and transducer.
The international journal of biochemistry & cell biology, 2008
Negative charged threonine 95 of c-Jun is essential for c-Jun N-terminal kinase-dependent phospho... more Negative charged threonine 95 of c-Jun is essential for c-Jun N-terminal kinase-dependent phosphorylation of threonine 91/93 and stress-induced c-Jun biological activity
Journal of Molecular Biology, 2003
Sensory rhodopsin II, a repellent phototaxis receptor from Natronobacterium pharaonis (NpSRII) fo... more Sensory rhodopsin II, a repellent phototaxis receptor from Natronobacterium pharaonis (NpSRII) forms a tight complex with its cognate transducer (NpHtrII). Light excitation of the receptor triggers conformational changes in both proteins, thereby activating the cellular two-component signalling cascade. In membranes, the two proteins form a 2:2 complex, which dissociates to a 1:1 heterodimer in micelles. Complexed to the transducer sensory rhodopsin II is no longer capable of light-driven proton pumping. In order to elucidate the dimerisation and the size of the receptor-binding domain of the transducer, isothermal titration calorimetry and electrophysiological experiments have been carried out. It is shown, that an N-terminal sequence of 114 amino acid residues is sufficient for tight binding (K d ¼ 240 nM; DH ¼ 217:6 kJ mol 21 ) and for inhibiting the proton transfer. These data and results obtained from selected sitedirected mutants indicate a synergistic interplay of transducer transmembrane domain (1 -82) and cytoplasmic peptide (83 -114) leading to an optimal and specific interaction between receptor and transducer.
The international journal of biochemistry & cell biology, 2008
Negative charged threonine 95 of c-Jun is essential for c-Jun N-terminal kinase-dependent phospho... more Negative charged threonine 95 of c-Jun is essential for c-Jun N-terminal kinase-dependent phosphorylation of threonine 91/93 and stress-induced c-Jun biological activity