Identification of potential amino acid residues supporting anticodon recognition in yeast methionyl-tRNA synthetase.

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 Lett

journal_title

FEBS letters

authors

Despons L,Walter P,Senger B,Ebel JP,Fasiolo F

doi

10.1016/0014-5793(91)81073-h

subject

Has Abstract

pub_date

1991-09-09 00:00:00

pages

217-20

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)81073-H

journal_volume

289

pub_type

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