ArfB can displace mRNA to rescue stalled ribosomes

J 2020

ArfB can displace mRNA to rescue stalled ribosomes

CARBONE, C.E., Gabriel DEMO, R. MADIREDDY, E. SVIDRITSKIY, A.A. KOROSTELEV et. al.

Základní údaje

Originální název

ArfB can displace mRNA to rescue stalled ribosomes

Autoři

CARBONE, C.E., Gabriel DEMO (703 Slovensko, garant, domácí), R. MADIREDDY, E. SVIDRITSKIY a A.A. KOROSTELEV

Vydání

Nature Communications, London, Nature Publishing Group, 2020, 2041-1723

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 14.919

Kód RIV

RIV/00216224:14740/20:00118225

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1038/s41467-020-19370-z

UT WoS

000591843300007

Klíčová slova anglicky

PEPTIDYL-TRANSFER-RNA; TRANSLATION TERMINATION; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; ESCHERICHIA-COLI; RELEASE; VISUALIZATION; MECHANISM; MOVEMENT; CODON

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 22. 2. 2021 11:53, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Ribosomes stalled during translation must be rescued to replenish the pool of translation-competent ribosomal subunits. Bacterial alternative rescue factor B (ArfB) releases nascent peptides from ribosomes stalled on mRNAs truncated at the A site, allowing ribosome recycling. Prior structural work revealed that ArfB recognizes such ribosomes by inserting its C-terminal alpha -helix into the vacant mRNA tunnel. In this work, we report that ArfB can efficiently recognize a wider range of mRNA substrates, including longer mRNAs that extend beyond the A-site codon. Single-particle cryo-EM unveils that ArfB employs two modes of function depending on the mRNA length. ArfB acts as a monomer to accommodate a shorter mRNA in the ribosomal A site. By contrast, longer mRNAs are displaced from the mRNA tunnel by more than 20 angstrom and are stabilized in the intersubunit space by dimeric ArfB. Uncovering distinct modes of ArfB function resolves conflicting biochemical and structural studies, and may lead to re-examination of other ribosome rescue pathways, whose functions depend on mRNA lengths. Alternative rescue factor B (ArfB) is an enzyme that releases peptides from stalled ribosomes to allow ribosome recycling. Here the authors carry-out cryo-EM analyses of 70S ribosomes complexed with ArfB on either a short or longer mRNA to reveal distinct modes of ArfB function.

Citovat

CARBONE, C.E., Gabriel DEMO, R. MADIREDDY, E. SVIDRITSKIY a A.A. KOROSTELEV. ArfB can displace mRNA to rescue stalled ribosomes. Nature Communications. London: Nature Publishing Group, 2020, roč. 11, č. 1, s. 5552-5560. ISSN 2041-1723. Dostupné z: https://dx.doi.org/10.1038/s41467-020-19370-z.

@article{1744936,
   author = {Carbone, C.E. and Demo, Gabriel and Madireddy, R. and Svidritskiy, E. and Korostelev, A.A.},
   article_location = {London},
   article_number = {1},
   doi = {http://dx.doi.org/10.1038/s41467-020-19370-z},
   keywords = {PEPTIDYL-TRANSFER-RNA; TRANSLATION TERMINATION; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; ESCHERICHIA-COLI; RELEASE; VISUALIZATION; MECHANISM; MOVEMENT; CODON},
   language = {eng},
   issn = {2041-1723},
   journal = {Nature Communications},
   title = {ArfB can displace mRNA to rescue stalled ribosomes},
   url = {https://www.nature.com/articles/s41467-020-19370-z.pdf},
   volume = {11},
   year = {2020}
}

TY  - JOUR
ID  - 1744936
AU  - Carbone, C.E. - Demo, Gabriel - Madireddy, R. - Svidritskiy, E. - Korostelev, A.A.
PY  - 2020
TI  - ArfB can displace mRNA to rescue stalled ribosomes
JF  - Nature Communications
VL  - 11
IS  - 1
SP  - 5552
EP  - 5552
PB  - Nature Publishing Group
SN  - 20411723
KW  - PEPTIDYL-TRANSFER-RNA
KW  - TRANSLATION TERMINATION
KW  - CRYSTAL-STRUCTURE
KW  - STRUCTURAL BASIS
KW  - ESCHERICHIA-COLI
KW  - RELEASE
KW  - VISUALIZATION
KW  - MECHANISM
KW  - MOVEMENT
KW  - CODON
UR  - https://www.nature.com/articles/s41467-020-19370-z.pdf
N2  - Ribosomes stalled during translation must be rescued to replenish the pool of translation-competent ribosomal subunits. Bacterial alternative rescue factor B (ArfB) releases nascent peptides from ribosomes stalled on mRNAs truncated at the A site, allowing ribosome recycling. Prior structural work revealed that ArfB recognizes such ribosomes by inserting its C-terminal alpha -helix into the vacant mRNA tunnel. In this work, we report that ArfB can efficiently recognize a wider range of mRNA substrates, including longer mRNAs that extend beyond the A-site codon. Single-particle cryo-EM unveils that ArfB employs two modes of function depending on the mRNA length. ArfB acts as a monomer to accommodate a shorter mRNA in the ribosomal A site. By contrast, longer mRNAs are displaced from the mRNA tunnel by more than 20 angstrom and are stabilized in the intersubunit space by dimeric ArfB. Uncovering distinct modes of ArfB function resolves conflicting biochemical and structural studies, and may lead to re-examination of other ribosome rescue pathways, whose functions depend on mRNA lengths. Alternative rescue factor B (ArfB) is an enzyme that releases peptides from stalled ribosomes to allow ribosome recycling. Here the authors carry-out cryo-EM analyses of 70S ribosomes complexed with ArfB on either a short or longer mRNA to reveal distinct modes of ArfB function.
ER  -

CARBONE, C.E., Gabriel DEMO, R. MADIREDDY, E. SVIDRITSKIY a A.A. KOROSTELEV. ArfB can displace mRNA to rescue stalled ribosomes. \textit{Nature Communications}. London: Nature Publishing Group, 2020, roč.~11, č.~1, s.~5552-5560. ISSN~2041-1723. Dostupné z: https://dx.doi.org/10.1038/s41467-020-19370-z.

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