期刊名称:Proceedings of the National Academy of Sciences
印刷版ISSN:0027-8424
电子版ISSN:1091-6490
出版年度:1975
卷号:72
期号:9
页码:3369-3373
DOI:10.1073/pnas.72.9.3369
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:In a temperature-sensitive mutant of E. coli defective in tRNA biosynthesis, many tRNA precursors, including monomeric and multimeric forms, accumulate. Some of the multimeric precursors contain three or more tRNA sequences within a molecule. These large precursors were cleaved by cell extracts first into intermediate size pieces which were subsequently processed by RNase P. On the basis of heat stability of mutant cell extracts, the endonuclease responsible for the initial cleavage appears to be distinct from RNase P and is designated RNase O. One of the monomeric precursors was shown to be processed first by RNase P and the product subsequently cleaved further into a smaller molecule. The nuclease responsible for this second cleavage also appears to be distinct from RNase P and is designated RNase Q. The functions of these nucleases are sequential in the trimming process with respect to that of RNase P; RNase O works prior to RNase P and RNase Q after RNase P but in both cases, not vice versa.