In vitro evolution of new ribozymes with polynucleotide kinase activity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-09

AUTHORS

J R Lorsch, J W Szostak

ABSTRACT

We have isolated a large number of polynucleotide kinase ribozymes from a pool of RNA molecules consisting of an ATP-binding domain flanked by regions of random sequence. Different classes of kinases catalyse the transfer of the gamma-thiophosphate of ATP-gamma S to the 5'-hydroxyl or to internal 2'-hydroxyls. An engineered version of one class is able to catalyse the transfer of thiophosphate from ATP-gamma S to the 5'-hydroxyl of an exogenous oligoribonucleotide substrate with multiple turnover, thus acting as a true enzyme. More... »

PAGES

31-36

Journal

TITLE

Nature

ISSUE

6492

VOLUME

371

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/371031a0

DOI

http://dx.doi.org/10.1038/371031a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1012863186

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7521014


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