RNase E enzymes from rhodobacter capsulatus and Escherichia coli differ in context- and sequence-dependent in vivo cleavage within the polycistronic puf mRNA |
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Authors: | Heck C Evguenieva-Hackenberg E Balzer A Klug G |
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Affiliation: | Institut für Mikrobiologie und Molekularbiologie, D-35392 Giessen, Germany. |
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Abstract: | The 5' pufQ mRNA segment and the pufLMX mRNA segment of Rhodobacter capsulatus exhibit different stabilities. Degradation of both mRNA segments is initiated by RNase E-mediated endonucleolytic cleavage. While Rhodobacter RNase E does not discriminate between the different sequences present around the cleavage sites within pufQ and pufL, Escherichia coli RNase E shows preference for the sequence harboring more A and U residues. |
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