Abstract
Ribosomal protein S1 is shown to interact with the non-coding RNA DsrA and with rpoS mRNA. DsrA is a non-coding RNA that is important in controlling expression of the rpoS gene product in Escherichia coli. Photochemical crosslinking, quadrupole-time of flight tandem mass spectrometry, and peptide sequencing have identified an interaction between DsrA and S1 in the 30S ribosomal subunit. Purified S1 binds both DsrA (K(obs) approximately 6 x 10(6) M(-1)) and rpoS mRNA (K(obs) approximately 3 x 10(7) M(-1)). Ribonuclease probing experiments indicate that S1 binding has a weak but detectable effect on the secondary structure of DsrA or rpoS mRNA.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / genetics*
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Base Sequence
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Electrophoretic Mobility Shift Assay
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Escherichia coli Proteins / metabolism*
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Mass Spectrometry
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Molecular Sequence Data
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Peptide Fragments / chemistry
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RNA, Messenger / metabolism*
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RNA, Small Untranslated
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RNA, Untranslated / metabolism*
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Ribonuclease, Pancreatic / metabolism
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Ribosomal Proteins / metabolism*
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Sigma Factor / genetics*
Substances
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Bacterial Proteins
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DsrA RNA, E coli
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Escherichia coli Proteins
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Peptide Fragments
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RNA, Messenger
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RNA, Small Untranslated
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RNA, Untranslated
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Ribosomal Proteins
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Sigma Factor
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ribosomal protein S1
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sigma factor KatF protein, Bacteria
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Ribonuclease, Pancreatic