Eukaryotic TYW1 Is a Radical SAM Flavoenzyme.

ABSTRACT: TYW1 is a radical S-adenosyl-l-methionine (SAM) enzyme that catalyzes the condensation of pyruvate and N-methylguanosine-containing tRNA^Phe, forming 4-demethylwyosine-containing tRNA^Phe. Homologues of TYW1 are found in both archaea and eukarya; archaeal homologues consist of a single domain, while eukaryal homologues contain a flavin binding domain in addition to the radical SAM domain shared with archaeal homologues. In this study, TYW1 from Saccharomyces cerevisiae (ScTYW1) was heterologously expressed in Escherichia coli and purified to homogeneity. ScTYW1 is purified with 0.54 ± 0.07 and 4.2 ± 1.9 equiv of flavin mononucleotide (FMN) and iron, respectively, per mole of protein, suggesting the protein is ∼50% replete with F

SUBMITTER: Young AP 

PROVIDER: S-EPMC8941971 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature