MinD-RNase E interplay controls localization of polar mRNAs in E. coli

Shanmugapriya Kannaiah; Omer Goldberger; Nawsad Alam; Georgina Barnabas; Yair Pozniak; Anat Nussbaum-Shochat; Ora Schueler-Furman; Tamar Geiger; Orna Amster-Choder

doi:10.1038/s44318-023-00026-9

MinD-RNase E interplay controls localization of polar mRNAs in E. coli

Shanmugapriya Kannaiah, Omer Goldberger, Nawsad Alam, Georgina Barnabas, Yair Pozniak, Anat Nussbaum-Shochat, Ora Schueler-Furman, Tamar Geiger, Orna Amster-Choder

Tel Aviv University, Weizmann Institute of Science, The Hebrew University of Jerusalem

Research output: Contribution to journal › Article › peer-review

Abstract

(Figure presented.) A subset of E. coli transcripts localizes to the cell poles via an unknown mechanism. Here, the interaction of MinD and RNase E is shown to prevent site-specific degradation of polar mRNAs, thus favoring their enrichment in the cell poles. Candidate approach and proteomic analysis identify MinD and RNase E as regulators of polar mRNA localization. MinD interacts with a short peptide within the membrane-targeting sequence of RNase E. In the absence of MinD, RNase E transiently accumulates at cell poles. Polar accumulation of RNase E in ΔminCDE cells destabilizes polar mRNAs, resulting in their elimination from the poles and potentially affecting localization of the encoded proteins.

Original language	English
Pages (from-to)	637-662
Number of pages	26
Journal	EMBO Journal
Volume	43
Issue number	4
Early online date	19 Jan 2024
DOIs	https://doi.org/10.1038/s44318-023-00026-9
State	Published - 15 Feb 2024

Keywords

Bacterial Cell Organization
Bacterial Cell Poles
MinD
RNA Localization
RNase E

All Science Journal Classification (ASJC) codes

General Neuroscience
Molecular Biology
General Biochemistry,Genetics and Molecular Biology
General Immunology and Microbiology

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10.1038/s44318-023-00026-9

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title = "MinD-RNase E interplay controls localization of polar mRNAs in E. coli",

abstract = "(Figure presented.) A subset of E. coli transcripts localizes to the cell poles via an unknown mechanism. Here, the interaction of MinD and RNase E is shown to prevent site-specific degradation of polar mRNAs, thus favoring their enrichment in the cell poles. Candidate approach and proteomic analysis identify MinD and RNase E as regulators of polar mRNA localization. MinD interacts with a short peptide within the membrane-targeting sequence of RNase E. In the absence of MinD, RNase E transiently accumulates at cell poles. Polar accumulation of RNase E in ΔminCDE cells destabilizes polar mRNAs, resulting in their elimination from the poles and potentially affecting localization of the encoded proteins.",

keywords = "Bacterial Cell Organization, Bacterial Cell Poles, MinD, RNA Localization, RNase E",

author = "Shanmugapriya Kannaiah and Omer Goldberger and Nawsad Alam and Georgina Barnabas and Yair Pozniak and Anat Nussbaum-Shochat and Ora Schueler-Furman and Tamar Geiger and Orna Amster-Choder",

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doi = "10.1038/s44318-023-00026-9",

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TY - JOUR

T1 - MinD-RNase E interplay controls localization of polar mRNAs in E. coli

AU - Kannaiah, Shanmugapriya

AU - Goldberger, Omer

AU - Alam, Nawsad

AU - Barnabas, Georgina

AU - Pozniak, Yair

AU - Nussbaum-Shochat, Anat

AU - Schueler-Furman, Ora

AU - Geiger, Tamar

AU - Amster-Choder, Orna

N1 - Publisher Copyright: © The Author(s) 2024.

PY - 2024/2/15

Y1 - 2024/2/15

N2 - (Figure presented.) A subset of E. coli transcripts localizes to the cell poles via an unknown mechanism. Here, the interaction of MinD and RNase E is shown to prevent site-specific degradation of polar mRNAs, thus favoring their enrichment in the cell poles. Candidate approach and proteomic analysis identify MinD and RNase E as regulators of polar mRNA localization. MinD interacts with a short peptide within the membrane-targeting sequence of RNase E. In the absence of MinD, RNase E transiently accumulates at cell poles. Polar accumulation of RNase E in ΔminCDE cells destabilizes polar mRNAs, resulting in their elimination from the poles and potentially affecting localization of the encoded proteins.

AB - (Figure presented.) A subset of E. coli transcripts localizes to the cell poles via an unknown mechanism. Here, the interaction of MinD and RNase E is shown to prevent site-specific degradation of polar mRNAs, thus favoring their enrichment in the cell poles. Candidate approach and proteomic analysis identify MinD and RNase E as regulators of polar mRNA localization. MinD interacts with a short peptide within the membrane-targeting sequence of RNase E. In the absence of MinD, RNase E transiently accumulates at cell poles. Polar accumulation of RNase E in ΔminCDE cells destabilizes polar mRNAs, resulting in their elimination from the poles and potentially affecting localization of the encoded proteins.

KW - Bacterial Cell Organization

KW - Bacterial Cell Poles

KW - MinD

KW - RNA Localization

KW - RNase E

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U2 - 10.1038/s44318-023-00026-9

DO - 10.1038/s44318-023-00026-9

M3 - مقالة

C2 - 38243117

SN - 0261-4189

VL - 43

SP - 637

EP - 662

JO - EMBO Journal

JF - EMBO Journal

IS - 4

ER -

MinD-RNase E interplay controls localization of polar mRNAs in E. coli

Abstract

Keywords

All Science Journal Classification (ASJC) codes

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