Mechanistic insights into the alternative ribosome recycling by HflXr

SM Seely, RS Basu, MG Gagnon - Nucleic Acids Research, 2024 - academic.oup.com
During stress conditions such as heat shock and antibiotic exposure, ribosomes stall on
messenger RNAs, leading to inhibition of protein synthesis. To remobilize ribosomes …

HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions

Y Zhang, CS Mandava, W Cao, X Li, D Zhang… - Nature structural & …, 2015 - nature.com
Adverse cellular conditions often lead to nonproductive translational stalling and arrest of
ribosomes on mRNAs. Here, we used fast kinetics and cryo-EM to characterize Escherichia …

Mechanisms of ribosome recycling in bacteria and mitochondria: a structural perspective

SM Seely, MG Gagnon - RNA biology, 2022 - Taylor & Francis
In all living cells, the ribosome translates the genetic information carried by messenger
RNAs (mRNAs) into proteins. The process of ribosome recycling, a key step during protein …

Structural basis for HflXr-mediated antibiotic resistance in Listeria monocytogenes

TO Koller, KJ Turnbull, K Vaitkevicius… - Nucleic Acids …, 2022 - academic.oup.com
HflX is a ubiquitous bacterial GTPase that splits and recycles stressed ribosomes. In addition
to HflX, Listeria monocytogenes contains a second HflX homolog, HflXr. Unlike HflX, HflXr …

A new mechanism for ribosome rescue can recruit RF1 or RF2 to nonstop ribosomes

TDP Goralski, GS Kirimanjeswara, KC Keiler - MBio, 2018 - Am Soc Microbiol
Bacterial ribosomes frequently translate to the 3′ end of an mRNA without terminating at an
in-frame stop codon. In all bacteria studied to date, these “nonstop” ribosomes are rescued …

The universally conserved GTPase HflX is an RNA helicase that restores heat-damaged Escherichia coli ribosomes

S Dey, C Biswas, J Sengupta - Journal of Cell Biology, 2018 - rupress.org
The ribosome-associated GTPase HflX acts as an antiassociation factor upon binding to the
50S ribosomal subunit during heat stress in Escherichia coli. Although HflX is recognized as …

Disassembly of the Staphylococcus aureus hibernating 100S ribosome by an evolutionarily conserved GTPase

A Basu, MNF Yap - Proceedings of the National Academy of …, 2017 - National Acad Sciences
The bacterial hibernating 100S ribosome is a poorly understood form of the dimeric 70S
particle that has been linked to pathogenesis, translational repression, starvation responses …

[HTML][HTML] E. coli HflX interacts with 50S ribosomal subunits in presence of nucleotides

N Jain, N Dhimole, AR Khan, D De, SK Tomar… - Biochemical and …, 2009 - Elsevier
HflX is a GTP binding protein of unknown function. Based on the presence of the hflX gene
in hflA operon, HflX was believed to be involved in the lytic-lysogenic decision during phage …

Hibernation factors directly block ribonucleases from entering the ribosome in response to starvation

T Prossliner, K Gerdes, MA Sørensen… - Nucleic Acids …, 2021 - academic.oup.com
Ribosome hibernation is a universal translation stress response found in bacteria as well as
plant plastids. The term was coined almost two decades ago and despite recent insights …

Post-termination ribosome intermediate acts as the gateway to ribosome recycling

A Prabhakar, MC Capece, A Petrov, J Choi, JD Puglisi - Cell reports, 2017 - cell.com
During termination of translation, the nascent peptide is first released from the ribosome,
which must be subsequently disassembled into subunits in a process known as ribosome …