TYW1: A Radical SAM Enzyme Involved in the Biosynthesis of Wybutosine Bases

Transfer RNA is extensively modified by the actions of a variety of enzymes. The radical S-adenosyl-l-methionine enzyme TYW1 modifies tRNA forming the characteristic tricyclic ring via the condensation of carbons 2 and 3 of pyruvate. This chapter details methods that are required for studies of TYW1...

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Veröffentlicht in:	Methods in enzymology 2018, Vol.606, p.119-153
Hauptverfasser:	Young, Anthony P, Bandarian, Vahe
Format:	Artikel
Sprache:	eng
Schlagworte:	Archaeal Proteins - genetics Archaeal Proteins - isolation & purification Archaeal Proteins - metabolism Carboxy-Lyases - genetics Carboxy-Lyases - isolation & purification Carboxy-Lyases - metabolism Enzyme Assays - methods Iron-Sulfur Proteins - genetics Iron-Sulfur Proteins - isolation & purification Iron-Sulfur Proteins - metabolism Methanocaldococcus - metabolism Nucleosides - metabolism Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism RNA, Transfer - metabolism S-Adenosylmethionine - metabolism Sequence Alignment
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Beschreibung
Zusammenfassung:	Transfer RNA is extensively modified by the actions of a variety of enzymes. The radical S-adenosyl-l-methionine enzyme TYW1 modifies tRNA forming the characteristic tricyclic ring via the condensation of carbons 2 and 3 of pyruvate. This chapter details methods that are required for studies of TYW1.
ISSN:	0076-6879 1557-7988
DOI:	10.1016/bs.mie.2018.04.024