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Cloning and characterization of the RNase P RNA genes from tow porcine mycoplasmas
Author(s) -
Svärd Staffan G.,
Mattsson Jens G.,
Johansson KarlErik,
Kirsebom Leif A.
Publication year - 1994
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1994.tb00363.x
Subject(s) - rnase p , biology , rnase h , rna , rnase mrp , degradosome , transcription (linguistics) , microbiology and biotechnology , non coding rna , gene , rnase ph , genetics , linguistics , philosophy
Summary We report the cloning of the RNase P RNA genes from the primary aetiological agent of porcine pneumonia, Mycoplasma hyopneumoniae , and the closely related commensal, Mycoplasma flocculare. The monocistronic genes each have promoters with AT‐rich ‐35 regions and Rho‐independent‐like transcription terminators which are retained in the RNase P RNA. Both of these RNase P RNA variants are shown to be catalytically active in vitro in spite of a low overall GC content (30%). Our results suggest a new example of a stable mini‐helix in the conserved core of the mycoplasmal RNase P RNAs. Deletion of the corresponding structural element in Escherichia coli RNase P RNA (M1 RNA) generated an RNase P RNA with an impaired substrate interaction. Displacement of this structural element with the mycoplasmal mini‐helix resulted in an enzyme with a phenotype similar to that of wild‐type M1 RNA. in addition, this structural element is important for lead ion‐induced cleavage at specific sites in M1 RNA.