Abstract
LytM is one kind of autolysin expressed in Staphylococcus aureus. It can hydrolyze peptide bond of pentaglycine, which is the component of cell wall. Until now, the regulation on the expression of LytM is still unclear. Here, we found that the level of LytM in the RNAIII mutant was increased. RNAIII is an important small regulatory RNA in S. aureus. Our further investigation revealed that RNAIII can interact with the 5'UTR of lytM mRNA and block the ribosome binding sites [RBS]. So our results identified that LytM was the new target of RNAIII.
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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5' Untranslated Regions
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Bacterial Proteins / biosynthesis*
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Bacterial Proteins / genetics*
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Bacterial Proteins / metabolism
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Binding Sites
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Down-Regulation
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Endopeptidases / biosynthesis*
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Endopeptidases / genetics*
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Endopeptidases / metabolism
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N-Acetylmuramoyl-L-alanine Amidase / genetics
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N-Acetylmuramoyl-L-alanine Amidase / metabolism
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RNA, Bacterial / genetics*
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RNA, Bacterial / metabolism*
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RNA, Messenger / genetics
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Ribosomes / genetics
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Ribosomes / metabolism
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Staphylococcus aureus / genetics*
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Staphylococcus aureus / metabolism*
Substances
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5' Untranslated Regions
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Bacterial Proteins
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RNA, Bacterial
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RNA, Messenger
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RNAIII, Staphylococcus aureus
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Endopeptidases
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LytM protein, Staphylococcus aureus
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N-Acetylmuramoyl-L-alanine Amidase