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Anomalous RNA substrates for mammalian tRNA 3′ processing endoribonuclease
Author(s) -
Nashimoto Masayuki
Publication year - 2000
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/s0014-5793(00)01462-9
Subject(s) - endoribonuclease , rna , cleave , transfer rna , cleavage (geology) , biology , biochemistry , base pair , enzyme , chemistry , microbiology and biotechnology , rnase p , dna , gene , paleontology , fracture (geology)
Mammalian tRNA 3′ processing endoribonuclease (3′ tRNase) is an enzyme responsible for the removal of a 3′ trailer from pre‐tRNA. The enzyme can also recognize and cleave any target RNA that forms a pre‐tRNA‐like complex with another RNA. To investigate the interaction between 3′ tRNase and substrates, we tested various anomalous pre‐tRNA‐like complexes for cleavage by pig 3′ tRNase. We examined how base mismatches in the acceptor stem affect 3′ tRNase cleavage of RNA complexes, and found that even one base mismatch in the acceptor stem drastically reduces the cleavage efficiency. Mammalian 3′ tRNase was able to recognize complexes between target RNAs and 5′‐half tDNAs, and cleave the target RNAs, although inefficiently, whereas the enzyme had no activity to cleave phosphodiester bonds of DNA. A relatively long RNA target, the Escherichia coli chloramphenicol acetyltransferase (CAT) mRNA, was cleaved by 3′ tRNase in the presence of appropriate 5′‐half tRNAs. We also demonstrated that an RNA complex of lin‐4 and lin‐14 from Caenorhabditis elegans can be recognized and cleaved by pig 3′ tRNase.