Filtern
Volltext vorhanden
- ja (5)
Gehört zur Bibliographie
- ja (5)
Dokumenttyp
Sprache
- Englisch (5)
Schlagworte
- Chlamydia (1)
- Chlamydia trachomatis (1)
- III secretion system (1)
- Legionella (1)
- Meningitis (1)
- Mycobacterium (1)
- Mycobacterium tuberculosis (1)
- Neisseria gonorrhoeae (1)
- Neisseria meningitidis (1)
- Pathogens (1)
- RNAlater (1)
- Salmonella (1)
- Simkania (1)
- Simkania negevensis (1)
- acid (1)
- allelic replacement (1)
- antitermination (1)
- bacterium Legionella pneumophila (1)
- endocytic multivesicular bodies (1)
- endoplasmic reticulum (1)
- endoribonuclease (1)
- expression (1)
- flash freezing (1)
- genome sequencing (1)
- geometry (1)
- host pathogen interactions (1)
- immuno-magnetic purification (1)
- intracellular bacteria (1)
- mammalian genomics (1)
- mechanism (1)
- men who have sex with men (1)
- meningococcal disease (1)
- metagenomics (1)
- metaproteomics (1)
- microbiome (1)
- microbiota (1)
- mouse models (1)
- nitrites (1)
- pathogen vacuole (1)
- phagosome maturation arrest (1)
- proteins (1)
- proteomics (1)
- sample storage (1)
- spectrometry-based proteomics (1)
- transcription (1)
- translation (1)
Institut
EU-Projektnummer / Contract (GA) number
- 278864 (1)
In Staphylococcus aureus, de novo methionine biosynthesis is regulated by a unique hierarchical pathway involving stringent-response controlled CodY repression in combination with a T-box riboswitch and RNA decay. The T-box riboswitch residing in the 5′ untranslated region (met leader RNA) of the S. aureus metICFE-mdh operon controls downstream gene transcription upon interaction with uncharged methionyl-tRNA. met leader and metICFE-mdh (m)RNAs undergo RNase-mediated degradation in a process whose molecular details are poorly understood. Here we determined the secondary structure of the met leader RNA and found the element to harbor, beyond other conserved T-box riboswitch structural features, a terminator helix which is target for RNase III endoribonucleolytic cleavage. As the terminator is a thermodynamically highly stable structure, it also forms posttranscriptionally in met leader/ metICFE-mdh read-through transcripts. Cleavage by RNase III releases the met leader from metICFE-mdh mRNA and initiates RNase J-mediated degradation of the mRNA from the 5′-end. Of note, metICFE-mdh mRNA stability varies over the length of the transcript with a longer lifespan towards the 3′-end. The obtained data suggest that coordinated RNA decay represents another checkpoint in a complex regulatory network that adjusts costly methionine biosynthesis to current metabolic requirements.