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Characterization of the newly constructed domains that replace P5abc within the Tetrahymena ribozyme
Author(s) -
Ikawa Yoshiya,
Shiraishi Hideaki,
Inoue Tan
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00918-0
Subject(s) - ribozyme , tetrahymena , vs ribozyme , mammalian cpeb3 ribozyme , activator (genetics) , hairpin ribozyme , microbiology and biotechnology , biology , function (biology) , chemistry , computational biology , biophysics , biochemistry , rna , gene
The P5abc domain of the Tetrahymena ribozyme has been shown to function as an activator that enhances core catalytic activity of the ribozyme. We reported previously that several new domains in that their primary sequences are different from that of P5abc are also capable of activating the ribozyme. It was unclear whether the mechanism of activation by the new domains is identical to that by P5abc. We have investigated structural and functional properties of the new domains and obtained evidence that strongly indicates that a particular domain activates the ribozyme in a different manner from that by P5abc.