Reconstitution of enzymatic activity from fragments of M1 RNA

C. Guerrier-Takada, Sidney Altman

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

Certain fragments of M1 RNA, the catalytic subunit of RNase P from Escherichia coli, either have no enzymatic activity at all or have altered substrate specificity compared with that of the intact catalytic RNA. After simple mixing in vitro, many of these fragments of M1 RNA can reassociate with other fragments to form complexes that have enzymatic activity typical of wild-type M1 RNA. Furthermore, inactive M1 RNA molecules with internal deletions can be complemented in vitro by other inactive derivatives of M1 RNA that have nonoverlapping deletions. Thus, two inactive molecules of M1 RNA can interact to form an active RNA enzyme. Functional attributes can be assigned to various regions of M1 RNA when the reconstitution process is combined with assays for activity with different substrates.

Original languageEnglish (US)
Pages (from-to)1266-1270
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number4
StatePublished - 1992
Externally publishedYes

Fingerprint

RNA
Ribonuclease P
Catalytic RNA
Substrate Specificity
Catalytic Domain
Escherichia coli
Enzymes
In Vitro Techniques

Keywords

  • RNA catalysis
  • RNA-RNA complementation
  • RNA-RNA interaction
  • RNase P

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Reconstitution of enzymatic activity from fragments of M1 RNA. / Guerrier-Takada, C.; Altman, Sidney.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, No. 4, 1992, p. 1266-1270.

Research output: Contribution to journalArticle

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