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Published July 1983 | public
Journal Article

RNA ligase in bacteria: Formation of a 2′,5′ linkage by an E. coli extract

Abstract

Ligase activity was detected in extracts of Escherichia coli, Clostridium tartarivorum, Rhodospirillum salexigens, Chromatium gracile, and Chlorobium limicola. Ligase was measured by joining of tRNA halves produced from yeast IVS-containing tRNA precursors by a yeast endonuclease. The structure of tRNA^(Tyr) halves joined by an E. coli extract was examined. The ligated junction is resistant to nuclease P1 and RNAase T2 but sensitive to venom phosphodiesterase and alkaline hydrolysis, consistent with a 2′,5′ linkage. The nuclease-resistant junction dinucleotide comigrates with authentic (2′,5′) A^PA marker in thin-layer chromatography. The phosphate in the newly formed phosphodiester bond is derived from the pre-tRNA substrate. The widespread existence of a bacterial ligase raises the possibility of a novel class of RNA processing reactions.

Additional Information

© 1983 MIT. Received April 20, 1983. We would especially like to acknowledge the talented technical assistance of Miriam Wright. We thank Richard Ogden and Peter Gegenheimer for their ongoing support of all aspects of this work and Richard Schwartz for a critical reading of the manuscript. This work was supported by grants from the American Cancer Society and the National Institutes of Health. C. L. G. was the recipient of a postdoctoral fellowship from the American Cancer Society. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18' U.S.C. Section 1734 solely to indicate this fact.

Additional details

Created:
August 19, 2023
Modified:
October 25, 2023