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Mutations affecting two distinct functions of the RNA component of RNase P.
Author(s) -
Shiraishi H.,
Shimura Y.
Publication year - 1986
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1986.tb04698.x
Subject(s) - rna , biology , rnase p , mutant , rna editing , post transcriptional modification , rnase h , microbiology and biotechnology , gene , genetics
The effect of structural changes on the functions of the RNA component (M1 RNA) of ribonuclease P (RNase P) of Escherichia coli has been studied using the thermosensitive mutants of the rnpB gene. One of the mutants, ts709, has two G‐‐A substitutions at positions 89 and 365 from the 5′ end of M1 RNA. Of these substitutions, the one at position 89 from the 5′ end is responsible for the phenotype of this mutant. Although the RNase P activity of ts709 is thermosensitive, the mutant M1 RNA has the same catalytic activity as the wild‐type RNA. M1 RNA of another mutant, ts2418, has a G‐‐A substitution at position 329. This mutant RNA has extremely low catalytic activity. The upstream mutational site of ts709 appears to play a role in the association with the protein subunit, whereas the mutational site of ts2418 is related to the catalytic function of M1 RNA.