Mechanistic insights into the alternative ribosome recycling by HflXr
During stress conditions such as heat shock and antibiotic exposure, ribosomes stall on
messenger RNAs, leading to inhibition of protein synthesis. To remobilize ribosomes …
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 …
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 …
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 …
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 …
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 …
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
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 …
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 …
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 …
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
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 …
which must be subsequently disassembled into subunits in a process known as ribosome …