Covalent aspartylation of aspartyl-tRNA synthetase from Bakers' yeast by its cognat aspartyl adenylate: identification of the labeled residues

Journal Article · Tue Apr 07 00:00:00 EDT 1987 · Biochemistry; (United States)

OSTI ID:5942546

Mejdoub, H; Kern, D; Giege, R; Ebel, J P; Boulanger, Y; Reinbolt, J

Aspartyl-tRNA synthetase from bakers' yeast gives an unstable complex with the cognate adenylate, which reacts after dissociation with amino acid side chains of the protein. This leads to a covalent incorporation of (/sup 14/C)-aspartic acid into aspartyl-tRNA synthetase via amide or ester bonds formed between the ..cap alpha..-carboxyl group of activated aspartic acid and accessible lysines, serines, and threonines. This property is used to label the peptides at the surface of the enzyme. The main labeled residues have been identified, and their location in the primary structure is discussed in relation to structural properties of aspartyl-tRNA synthetase.

• Research Organization: CNRS, Strasbourg, France
• OSTI ID: 5942546
• Journal Information: Biochemistry; (United States), Vol. 26:7
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
LIGASES
BIOCHEMISTRY
LABELLING
ADENYLIC ACID
AMINO ACID SEQUENCE
ASPARTIC ACID
CARBON 14 COMPOUNDS
LIQUID COLUMN CHROMATOGRAPHY
SCINTILLATION COUNTING
TRANSFER RNA
YEASTS
AMINO ACIDS
CARBOXYLIC ACIDS
CHEMISTRY
CHROMATOGRAPHY
COUNTING TECHNIQUES
ENZYMES
FUNGI
LABELLED COMPOUNDS
MICROORGANISMS
MOLECULAR STRUCTURE
NUCLEIC ACIDS
NUCLEOTIDES
ORGANIC ACIDS
ORGANIC COMPOUNDS
PLANTS
RNA
SEPARATION PROCESSES
550201* - Biochemistry- Tracer Techniques