Dynamic Membrane Localization of RNase Y in Bacillus subtilis

RNase MRP RNase PH Transcription RNase H Cleavage (geology) Inner membrane Ribonuclease III
DOI: 10.1128/mbio.03337-19 Publication Date: 2020-02-17T13:09:17Z
ABSTRACT
Metabolic turnover of mRNA is fundamental to the control gene expression in all organisms, notably fast-adapting prokaryotes. In many bacteria, RNase Y initiates global decay via an endonucleolytic cleavage, as shown Gram-positive model organism Bacillus subtilis This enzyme tethered inner cell membrane, a pseudocompartmentalization coherent with its task initiating cleavage/maturation mRNAs that are translated at periphery. Here, we used total internal reflection fluorescence microscopy (TIRFm) and single-particle tracking (SPT) visualize analyze distribution dynamics living cells. We find diffuses rapidly membrane form dynamic short-lived foci. Unlike E, major decay-initiating Escherichia coli, formation foci not dependent on presence RNA substrates. On contrary, become more abundant increase size following transcription arrest, suggesting they do constitute most active nuclease. The Y-complex three proteins (YaaT, YlbF, YmcA) has previously been play important role for activity vivo demonstrate mutations have effect similar but much stronger than depletion increasing number membrane. Our data suggest shifts assembly status toward fewer smaller complexes, thereby cleavage efficiency complex substrates like polycistronic mRNAs.IMPORTANCE All organisms must degrade adapt changing environments. initiation generally occurs through cleavage. probably other key this Y, which anchored While appears translation occurring primarily periphery, our knowledge cells very scarce. show moves along These contrasts E. where it was also protein (Y-complex) known influence specificity capable shifting complexes. highlights differences between E- Y-based degradation machineries.
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