- Transcript-specific selective translation by specialized ribosomes bearing genome-encoded heterogeneous rRNAs in V. vulnificus CMCP6
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Younkyung Choi , Minju Joo , Wooseok Song , Minho Lee , Hana Hyeon , Hyun-Lee Kim , Ji-Hyun Yeom , Kangseok Lee , Eunkyoung Shin
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J. Microbiol. 2022;60(12):1162-1167. Published online November 24, 2022
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DOI: https://doi.org/10.1007/s12275-022-2437-9
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Ribosomes composed of genome-encoded heterogeneous
rRNAs are implicated in the rapid adaptation of bacterial
cells to environmental changes. A previous study showed that
ribosomes bearing the most heterogeneous rRNAs expressed
from the rrnI operon (I-ribosomes) are implicated in the preferential
translation of a subset of mRNAs, including hspA
and tpiA, in Vibrio vulnificus CMCP6. In this study, we show
that HspA nascent peptides were predominantly bound to
I-ribosomes. Specifically, I-ribosomes were enriched more
than two-fold in ribosomes that were pulled down by immunoprecipitation
of HspA peptides compared with the proportion
of I-ribosomes in crude ribosomes and ribosomes pulled
down by immunoprecipitation of RNA polymerase subunit
ß peptides in the wild-type (WT) and rrnI-completed strains.
Other methods that utilized the incorporation of an affinity
tag in 23S rRNA or chimeric rRNA tethering 16S and 23S
rRNAs, which generated specialized functional ribosomes
in Escherichia coli, did not result in functional I-ribosomes
in V. vulnificus CMCP6. This study provides direct evidence
of the preferential translation of hspA mRNA by I-ribosomes.
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Citations
Citations to this article as recorded by  - Functional conservation of specialized ribosomes bearing genome-encoded variant rRNAs in Vibrio species
Younkyung Choi, Eunkyoung Shin, Minho Lee, Ji-Hyun Yeom, Kangseok Lee, Bashir Sajo Mienda
PLOS ONE.2023; 18(12): e0289072. CrossRef - Relaxed Cleavage Specificity of Hyperactive Variants of Escherichia coli RNase E on RNA I
Dayeong Bae, Hana Hyeon, Eunkyoung Shin, Ji-Hyun Yeom, Kangseok Lee
Journal of Microbiology.2023; 61(2): 211. CrossRef
- The α-Barrel Tip Region of Escherichia coli TolC Homologs of Vibrio vulnificus Interacts with the MacA Protein to Form the Functional Macrolide-Specific Efflux Pump MacAB-TolC
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Minho Lee , Hyun-Lee Kim , Saemee Song , Minju Joo , Seunghwa Lee , Daeyoung Kim , Yoonsoo Hahn , Nam-Chul Ha , Kangseok Lee
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J. Microbiol. 2013;51(2):154-159. Published online April 27, 2013
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DOI: https://doi.org/10.1007/s12275-013-2699-3
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890
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Abstract
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TolC and its homologous family of proteins are outer membrane factors that are essential for exporting small molecules and toxins across the outer membrane in Gram-negative bacteria. Two open reading frames in the Vibrio vulnificus genome that encode proteins homologous to Escherichia coli TolC, designated TolCV1 and TolCV2, have 51.3% and 29.6% amino acid identity to TolC, respectively. In this study, we show that TolCV1 and TolCV2 functionally and physically interacted with the membrane fusion protein, MacA, a component of the macrolide-specific MacAB-TolC pump of E. coli. We further show that the conserved residues located at the aperture tip region of the α-hairpin of TolCV1 and TolCV2 played an essential role in the formation of the functional MacAB-TolC pump using site-directed mutational analyses. Our findings suggest that these outer membrane factors have
conserved tip-to-tip interaction with the MacA membrane fusion protein for action of the drug efflux pump in Gramnegative bacteria.
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Citations
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TolCV1 inhibition by NPPB renders
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