Journal article

RNase E enzymes from Rhodobacter capsulatus and Escherichia coli differ in context- and sequence-dependent in vivo cleavage within the polycistronic puf mRNA


Authors listHeck, C; Evguenieva-Hackenberg, E; Balzer, A; Klug, G

Publication year1999

Pages7621-7625

JournalJournal of Bacteriology

Volume number181

Issue number24

ISSN0021-9193

URLhttps://jb.asm.org/content/181/24/7621

PublisherAmerican Society for Microbiology


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.



Authors/Editors




Citation Styles

Harvard Citation styleHeck, C., Evguenieva-Hackenberg, E., Balzer, A. and Klug, G. (1999) RNase E enzymes from Rhodobacter capsulatus and Escherichia coli differ in context- and sequence-dependent in vivo cleavage within the polycistronic puf mRNA, Journal of Bacteriology, 181(24), pp. 7621-7625. https://jb.asm.org/content/181/24/7621

APA Citation styleHeck, C., Evguenieva-Hackenberg, E., Balzer, A., & Klug, G. (1999). RNase E enzymes from Rhodobacter capsulatus and Escherichia coli differ in context- and sequence-dependent in vivo cleavage within the polycistronic puf mRNA. Journal of Bacteriology. 181(24), 7621-7625. https://jb.asm.org/content/181/24/7621


Last updated on 2025-21-05 at 13:14