Abstract:
:Sequence comparisons among methionyl-tRNA synthetases from different organisms reveal only one block of homology beyond the last beta strand of the mononucleotide fold. We have introduced a series of semi-conservative amino acid replacements in the conserved motif of yeast methionyl-tRNA synthetase. The results indicate that replacements of two polar residues (Asn584 and Arg588) affected specifically the aminoacylation reaction. The location of these residues in the tertiary structure of the enzyme is compatible with a direct interaction of the amino acid side-chains with the tRNA anticodon.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Despons L,Walter P,Senger B,Ebel JP,Fasiolo Fdoi
10.1016/0014-5793(91)81073-hsubject
Has Abstractpub_date
1991-09-09 00:00:00pages
217-20issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(91)81073-Hjournal_volume
289pub_type
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