Multiple structural flavors of RNase P in precursor tRNA processing
Wiley Interdisciplinary Reviews - RNA,
Год журнала:
2024,
Номер
15(2)
Опубликована: Март 1, 2024
The
precursor
transfer
RNAs
(pre-tRNAs)
require
extensive
processing
to
generate
mature
tRNAs
possessing
proper
fold,
structural
stability,
and
functionality
required
sustain
cellular
viability.
road
tRNA
maturation
follows
an
ordered
process:
5'-processing,
3'-processing,
modifications
at
specific
sites,
if
any,
3'-CCA
addition
before
aminoacylation
recruitment
the
protein
synthesis
machinery.
Ribonuclease
P
(RNase
P)
is
a
universally
conserved
endonuclease
in
all
domains
of
life,
performing
hydrolysis
pre-tRNA
sequences
5'
end
by
removal
phosphodiester
linkages
between
nucleotides
position
-1
+1.
Except
for
archaeal
species:
Nanoarchaeum
equitans
where
are
transcribed
from
leaderless-position
+1,
RNase
indispensable
life
displays
fundamental
variations
terms
enzyme
subunit
composition,
mechanism
substrate
recognition
active
site
architecture,
utilizing
cases
two
metal
ion-mediated
catalytic
reaction.
While
canonical
RNA-based
ribonucleoprotein
has
been
well-known
occur
bacteria,
archaea,
eukaryotes,
occurrence
RNA-free
protein-only
eukaryotes
homologs
Aquifex
prokaryotes
discovered
more
recently.
This
review
aims
provide
comprehensive
overview
diversity
displayed
various
holoenzymes
towards
harnessing
critical
RNA-protein
protein-protein
interactions
achieving
functionality.
Furthermore,
alternate
roles
functional
interchangeability
discussed
context
its
employability
several
clinical
biotechnological
applications.
article
categorized
under:
RNA
Processing
>
Evolution
Genomics
Ribonucleoprotein
Interactions
with
Proteins
Other
Molecules
RNA-Protein
Complexes.
Язык: Английский
Identification of Two Elusive Human Ribonuclease MRP-Specific Protein Components
Rui Che,
Bhoomi Mirani,
M. Yazdan Panah
и другие.
bioRxiv (Cold Spring Harbor Laboratory),
Год журнала:
2025,
Номер
unknown
Опубликована: Янв. 22, 2025
All
known
protein
components
of
one
the
longest-studied
human
ribonucleoprotein
ribozyme
nuclear
Ribonuclease
MRP
(RNase
MRP),
which
processes
pre-rRNA
at
ITS1
site
2,
are
shared
with
P
P),
cleaves
pre-tRNA
5'
leader
sequences.
Our
genome-wide
forward
genetic
screening
identified
two
poorly
characterized
genes,
we
named
RPP24
and
RPP64.
We
show
that
these
genes
required
for
2
processing
their
products
efficiently
associate
RNA
MRP.
Unlike
all
other
RNase
components,
RPP64
not
activity
do
P-specific
H1.
Despite
extremely
limited
sequence
homology,
exhibit
predicted
structural
similarities
to
MRP-specific
in
S.
cerevisiae
,
specific
differences
regions
substrate
recognition.
Collectively,
our
functional
validation
revealed
first
unique
Язык: Английский