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The 54 kDa RNA‐binding protein from mustard chloroplasts mediates endonucleolytic transcript 3′ end formation in vitro
Author(s) -
Nickelsen Jörg,
Link Gerhard
Publication year - 1993
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1993.03040537.x
Subject(s) - in vitro , microbiology and biotechnology , rna , rna binding protein , messenger rna , chloroplast , biology , chemistry , genetics , gene
A 54 kDa protein from mustard chloroplasts was previously shown to interact specifically with a conserved U‐rich sequence element in RNA derived from the 3′ flanking regions of the plastid trnK and rps16 genes, which code for tRNA Lys and ribosomal protein CS19, respectively (Nickelsen and Link, 1991). This RNA‐binding protein has now been purified by affinity chromatography on heparin Sepharose and poly(U) Sepharose. In vitro processing experiments and nuclease S1 analyses of the processing products revealed that the 54 kDa polypeptide is an endonuclease. The in vitro cleavage sites are consistent with the positions of corresponding transcript in vivo 3′ ends downstream of trnK and rps16 , suggesting that RNA 3′ end formation takes place endonucleolytically also in vivo .