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Transfer RNA recognition by class I lysyl‐tRNA synthetase from the Lyme disease pathogen Borrelia burgdorferi
Author(s) -
Ambrogelly Alexandre,
Frugier Magali,
Ibba Michael,
Söll Dieter,
Giegé Richard
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.04.001
Subject(s) - borrelia burgdorferi , transfer rna , aminoacylation , biology , escherichia coli , microbiology and biotechnology , genetics , rna , gene , antibody
Borrelia burgdorferi and other spirochetes contain a class I lysyl‐tRNA synthetase (LysRS), in contrast to most eubacteria that have a canonical class II LysRS. We analyzed tRNA Lys recognition by B. burgdorferi LysRS, using two complementary approaches. First, the nucleotides of B. burgdorferi tRNA Lys in contact with B. burgdorferi LysRS were determined by enzymatic footprinting experiments. Second, the kinetic parameters for a series of variants of the B. burgdorferi tRNA Lys were then determined during aminoacylation by B. burgdorferi LysRS. The identity elements were found to be mostly located in the anticodon and in the acceptor stem. Transplantation of the identified identity elements into the Escherichia coli tRNA Asp scaffold endowed lysylation activity on the resulting chimera, indicating that a functional B. burgdorferi lysine tRNA identity set had been determined.