We
investigated
the
role
of
nucleolar
protein
Treacle
in
organizing
and
regulating
nucleolus
human
cells.
Our
results
support
Treacle’s
ability
to
form
liquid-like
phase
condensates
through
electrostatic
interactions
among
molecules.
The
formation
these
biomolecular
is
crucial
for
segregating
fibrillar
centers
from
dense
component
ensuring
high
levels
ribosomal
RNA
(rRNA)
gene
transcription
accurate
rRNA
processing.
Both
central
C-terminal
domains
are
required
condensates.
initiation
separation
attributed
domain.
domain
characterized
by
repeated
stretches
alternatively
charged
amino
acid
residues
vital
condensate
stability.
Overexpression
mutant
forms
that
cannot
compromises
assembly
centers,
suppressing
disrupting
These
also
fail
recruit
DNA
topoisomerase
II
binding
1
(TOPBP1),
damage
response
nucleolus.
Cellular and Molecular Life Sciences,
Journal Year:
2025,
Volume and Issue:
82(1)
Published: Feb. 20, 2025
Liquid–liquid
phase
separation
(LLPS),
driven
by
dynamic,
low-affinity
multivalent
interactions
of
proteins
and
RNA,
results
in
the
formation
macromolecular
condensates
on
chromatin.
These
structures
are
likely
to
provide
high
local
concentrations
effector
factors
responsible
for
various
processes
including
transcriptional
regulation
DNA
repair.
In
particular,
enhancers,
super-enhancers,
promoters
serve
as
platforms
condensate
assembly.
current
paradigm,
enhancer-promoter
(EP)
interaction
could
be
interpreted
a
result
enhancer-
promoter-based
contact/fusion.
There
is
increasing
evidence
that
spatial
juxtaposition
enhancers
provided
loop
extrusion
(LE)
SMC
complexes.
Here,
we
propose
may
act
barriers
LE,
thereby
contributing
nuclear
contacts
between
regulatory
genomic
elements.
Nature Communications,
Journal Year:
2025,
Volume and Issue:
16(1)
Published: March 11, 2025
Abstract
During
mitosis,
chromosomes
condense
and
decondense
to
segregate
faithfully
undamaged.
The
exact
molecular
mechanisms
are
not
well
understood.
We
identify
the
DEAD-box
helicase
eIF4A1/2
as
a
critical
factor
in
this
process.
In
cell-free
condensation
assay
is
crucial
for
process,
relying
on
its
RNA-binding
ability
but
ATPase
activity.
Reducing
levels
cells
consistently
slows
down
chromatin
decondensation
during
nuclear
reformation.
Conversely,
increasing
concentration
mitotic
accelerates
their
decondensation.
absence
of
affects
perichromatin
layer,
which
surrounds
mitosis
consists
RNA
mainly
nucleolar
proteins.
vitro,
acts
an
chaperone,
dissociating
biomolecular
condensates
chaperone
activity
required
regulate
composition
fluidity
dynamic
reorganization
exit
mitosis.
We
investigated
the
role
of
nucleolar
protein
Treacle
in
organizing
and
regulating
nucleolus
human
cells.
Our
results
support
Treacle’s
ability
to
form
liquid-like
phase
condensates
through
electrostatic
interactions
among
molecules.
The
formation
these
biomolecular
is
crucial
for
segregating
fibrillar
centers
from
dense
component
ensuring
high
levels
rRNA
gene
transcription
accurate
processing.
Both
central
C-terminal
domains
are
required
condensates.
initiation
separation
attributed
domain.
domain
characterized
by
repeated
stretches
alternatively
charged
amino-acid
residues
vital
condensate
stability.
Overexpression
mutant
forms
that
cannot
compromises
assembly
centers,
suppressing
disrupting
These
also
fail
recruit
DNA
topoisomerase
II
binding
1
(TOPBP1),
damage
response
nucleolus.
We
investigated
the
role
of
nucleolar
protein
Treacle
in
organizing
and
regulating
nucleolus
human
cells.
Our
results
support
Treacle’s
ability
to
form
liquid-like
phase
condensates
through
electrostatic
interactions
among
molecules.
The
formation
these
biomolecular
is
crucial
for
segregating
fibrillar
centers
from
dense
component
ensuring
high
levels
ribosomal
RNA
(rRNA)
gene
transcription
accurate
rRNA
processing.
Both
central
C-terminal
domains
are
required
condensates.
initiation
separation
attributed
domain.
domain
characterized
by
repeated
stretches
alternatively
charged
amino
acid
residues
vital
condensate
stability.
Overexpression
mutant
forms
that
cannot
compromises
assembly
centers,
suppressing
disrupting
These
also
fail
recruit
DNA
topoisomerase
II
binding
1
(TOPBP1),
damage
response
nucleolus.