Erythromycin-induced ribosome stalling and RNase J1-mediated mRNA processing inBacillus subtilis
نویسندگان
چکیده
منابع مشابه
Mechanisms of SecM-mediated stalling in the ribosome.
Nascent-peptide modulation of translation is a common regulatory mechanism of gene expression. In this mechanism, while the nascent peptide is still in the exit tunnel of the ribosome, it induces translational pausing, thereby controlling the expression of downstream genes. One example is SecM, which inhibits peptide-bond formation in the ribosome's peptidyl transferase center (PTC) during its ...
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In bacteria, ribosome stalling during translation of ErmBL leader peptide occurs in the presence of the antibiotic erythromycin and leads to induction of expression of the downstream macrolide resistance methyltransferase ErmB. The lack of structures of drug-dependent stalled ribosome complexes (SRCs) has limited our mechanistic understanding of this regulatory process. Here we present a cryo-e...
متن کاملDksA guards elongating RNA polymerase against ribosome-stalling-induced arrest.
In bacteria, translation-transcription coupling inhibits RNA polymerase (RNAP) stalling. We present evidence suggesting that, upon amino acid starvation, inactive ribosomes promote rather than inhibit RNAP stalling. We developed an algorithm to evaluate genome-wide polymerase progression independently of local noise and used it to reveal that the transcription factor DksA inhibits promoter-prox...
متن کاملMiscoding-induced stalling of substrate translocation on the bacterial ribosome.
Directional transit of the ribosome along the messenger RNA (mRNA) template is a key determinant of the rate and processivity of protein synthesis. Imaging of the multistep translocation mechanism using single-molecule FRET has led to the hypothesis that substrate movements relative to the ribosome resolve through relatively long-lived late intermediates wherein peptidyl-tRNA enters the P site ...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 2008
ISSN: 0950-382X,1365-2958
DOI: 10.1111/j.1365-2958.2008.06370.x