Multiple nucleotide cofactor use by yeast ligase in tRNA splicing. Evidence for independent ATP- and GTP-binding sites

• Published in: The Journal of biological chemistry Vol. 268; no. 4; pp. 2444 - 2450
• Main Authors: Belford, H.G, Westaway, S.K, Abelson, J, Greer, C.L
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 05.02.1993
• Subjects: ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; ADENOSINE TRIPHOSPHATE; Adenosine Triphosphate - metabolism; ADENOSINTRIFOSFATO; ADN RECOMBINADO; ADN RECOMBINE; Analytical, structural and metabolic biochemistry; ARN DE TRANSFERENCIA; ARN DE TRANSFERT; Biological and medical sciences; CITOSINA; CYTOSINE; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; GENE; GENES; Guanosine Triphosphate - metabolism; LIGASAS; LIGASE; Ligases; NUCLEOTIDE; NUCLEOTIDOS; OXIDORREDUCTASAS; OXYDOREDUCTASE; Protein Conformation; Recombinant Fusion Proteins - metabolism; RNA Ligase (ATP) - metabolism; RNA Ligase (ATP) - ultrastructure; RNA Splicing; RNA, Fungal - metabolism; RNA, Transfer - metabolism; SACCHAROMYCES CEREVISIAE; URIDINA; URIDINE; Fungi; Ligase; GTP; Splicing; t-RNA; Enzyme; Ascomycetes; Binding site; ATP; Cofactor; Saccharomyces cerevisiae; Thallophyta

We have examined multiple cofactor usage by yeast tRNA ligase in splicing in vitro. The ligase mechanism of action requires expenditure of two molar equivalents of nucleotide cofactor per mole of tRNA product. Recent evidence (Westaway, S. K., Belford, H. G., Apostol, B. L., Abelson, J., and Greer,...