Abstract：
:The gene encoding the enzyme tyrosyl tRNA synthetase from Bacillus stearothermophilus has been systematically altered using synthetic oligonucleotides as mutagens. The construction of mutations has been facilitated by using strains of bacteria defective in mismatch repair and also by utilising a genetic marker in the M13 strain (such as an amber mutation, or an EcoK or EcoB site) which allows selection for the progeny of M13 replication derived from the minus (mutagenized) strand. Several mutations have been constructed in the ATP binding site to elucidate the roles of individual residues in catalysis and substrate binding and it has even been possible to construct mutants which have improved affinity for ATP. Mutations in various surface lysine and arginine residues have allowed us to identify potential contacts with the tRNA, and indicate that a cluster of basic residues close to the C-terminus of the enzyme probably makes important interactions with the tRNA.
journal_name
Biochimiejournal_title
Biochimieauthors
Bedouelle H,Carter P,Waye MM,Winter G,Lowe DM,Wilkinson AJ,Fersht ARdoi
10.1016/s0300-9084(85)80161-9subject
Has Abstractpub_date
1985-07-01 00:00:00pages
737-43issue
7-8eissn
0300-9084issn
1638-6183pii
S0300-9084(85)80161-9journal_volume
67pub_type
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