Protein Phosphorylation Nexus of Cyanobacterial Adaptation and Metabolism
Kinases and Phosphatases,
Journal Year:
2024,
Volume and Issue:
2(2), P. 209 - 223
Published: June 20, 2024
Protein
phosphorylation
serves
as
a
fundamental
regulatory
mechanism
to
modulate
cellular
responses
environmental
stimuli
and
plays
crucial
role
in
orchestrating
adaptation
metabolic
homeostasis
various
diverse
organisms.
In
cyanobacteria,
an
ancient
phylum
of
significant
ecological
biotechnological
relevance,
protein
emerges
central
axis
mediating
adaptive
that
are
essential
for
survival
growth.
This
exhaustive
review
thoroughly
explores
the
complex
terrain
cyanobacterial
metabolism,
illustrating
its
forms
functional
implications.
Commencing
with
overview
physiology
historical
trajectory
research
prokaryotes,
this
navigates
through
mechanisms
two-component
sensory
systems
their
interplay
phosphorylation.
Furthermore,
it
investigates
different
feeding
modes
cyanobacteria
highlights
between
photoautotrophy,
variables,
susceptibility
photo-inhibition.
The
elucidation
coordinating
light
harvesting
acquisition
inorganic
nutrients
underscores
importance
physiology.
novelty
by
synthesizing
existing
knowledge
proposing
future
trajectories,
thereby
contributing
deeper
regulation
Language: Английский
Herbicide Pretilachlor Impairs Biofertilizer Potential of Anabaena doliolum: Integrating Proteomic Responses, Nitrogen fixation, and Computational Analysis
Journal of Hazardous Materials,
Journal Year:
2025,
Volume and Issue:
unknown, P. 138673 - 138673
Published: May 1, 2025
Language: Английский
Celebrating Women in Proteomics and Metabolomics
Journal of Proteome Research,
Journal Year:
2024,
Volume and Issue:
23(8), P. 2675 - 2679
Published: Aug. 2, 2024
Language: Английский
The new phycobilisome linker protein ApcI regulates high light adaptation inSynechocystissp. PCC 6803
bioRxiv (Cold Spring Harbor Laboratory),
Journal Year:
2024,
Volume and Issue:
unknown
Published: Sept. 15, 2024
Abstract
Phycobilisomes
are
versatile
cyanobacterial
antenna
complexes
that
harvest
light
energy
to
drive
photosynthesis.
These
can
also
adapt
various
conditions,
dismantling
under
high
prevent
photo-oxidation
and
arranging
in
rows
low
increase
harvesting
efficiency.
Light
quality
influences
phycobilisome
structure
function,
as
observed
far-red
exposure.
Here
we
describe
a
new,
linker
protein,
ApcI
(previously
hypothetical
protein
sll1911),
expressed
specifically
red
light.
We
characterized
Synechocystis
sp.
PCC
6803
using
mutant
strain
analyses,
binding
experiments,
interaction
studies.
Mutation
of
apcI
conferred
tolerance
compared
wild
type
with
reduced
transfer
from
phycobilisomes
the
photosystems.
Binding
experiments
revealed
replaces
ApcG
at
membrane-facing
side
core
paralogous
C-terminal
domain.
Additionally,
N-terminal
extension
was
found
interact
photosystem
II.
Our
findings
highlight
importance
remodeling
for
adaptation
different
conditions.
The
characterization
provides
new
insights
into
mechanisms
by
which
cyanobacteria
optimize
light-harvesting
response
varying
environments.
Language: Английский