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3′‐end processing of precursor M1 RNA by the N‐terminal half of RNase E
Author(s) -
Sim Soyeong,
Kim Kwang-sun,
Lee Younghoon
Publication year - 2002
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(02)03345-8
Subject(s) - rnase p , cleavage (geology) , rna , chemistry , microbiology and biotechnology , rnase h , escherichia coli , messenger rna , biochemistry , biology , gene , paleontology , fracture (geology)
M1 RNA, the catalytic component of Escherichia coli RNase P, is derived from the 3′‐end processing of precursor M1 RNA, a major transcript of the rnpB gene. In this study, we investigated the mechanism of 3′‐end processing of M1 RNA using the recombinant N‐terminal half RNase E. The cleavage site preference of RNase E differed from that of the 40% ammonium sulfate precipitate (ASP‐40), a partially purified cell extract containing processing activity. However, the addition of a trace amount of ASP‐40 changed the cleavage site preference of RNase E to that of ASP‐40 suggesting the involvement of a soluble factor in cleavage site preference.