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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins*
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Endoribonucleases / metabolism*
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Escherichia coli / enzymology*
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Light-Harvesting Protein Complexes*
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Nucleic Acid Conformation
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Photosynthetic Reaction Center Complex Proteins / genetics
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Photosynthetic Reaction Center Complex Proteins / metabolism
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RNA, Messenger / metabolism*
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Rhodobacter capsulatus / enzymology*
Substances
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Bacterial Proteins
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Light-Harvesting Protein Complexes
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Photosynthetic Reaction Center Complex Proteins
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PufL protein, Bacteria
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RNA, Messenger
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Endoribonucleases
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ribonuclease E