N-tosyl-L-phenylalanylchloromethane reacts with cysteine 81 in the molecule of elongation factor Tu from Escherichia coli |
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| Authors: | Ji&#x í Jon k, Torben E. Petersen, Brian F.C. Clark,Ivan Rychlí k |
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| Affiliation: | 1. Institute of Molecular Genetics, Czechoslovak Academy of Sciences, Flemingovo n. 2, 16637 Prague 6, Czechoslovakia;2. Department of Molecular Biology, Aarhus University, C.F Møllers Allè 130, DK-8000 Aarhus C Denmark;3. Department of Chemistry, Aarhus University, Langelandsgade 140, DK-8000 Aarhus C, Denmark |
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| Abstract: | Elongation factor EF-Tu from Escherichia coli was labelled with N-[14C]tosyl-L-phenylalanylchloromethane, digested with trypsin and the peptides obtained separated by HPLC. The only radioactive peak recovered corresponded to tryptic peptide containing residues 75–98. Sequencing of the peptide by automated Edman degradation identified cysteine 81 as the site of N-tosyl-L-phenylalanylchloromethane modification. These results confirm the importance of this residue for the interaction with aminoacyl-tRNAs. |
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| Keywords: | Elongation factor EF-Tu Cysteine 81 Escherichia coli Modification by TPCK HPLC chromatography Tryptic peptide |
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