Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.1.26.9 (
ribonuclease
)
6,589
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The characteristic fold of a protein is the decisive factor for its biological function. However, small structural changes to amino acids can also affect their function, for example in the case of post-translational modification (PTM). Many different types of PTMs are known, but for some, including chlorination, studies elucidating their importance are limited. A recent study revealed that the YjgF/YER057c/
UK114
family (YjgF family) member RidA from
Escherichia coli
shows chaperone activity after chlorination. Thus, to identify the functional and structural differences of RidA upon chlorination, we studied an RidA homolog from
Staphylococcus aureus
: YabJ. The overall structure of
S. aureus
YabJ was similar to other members of the YjgF family, showing deep pockets on its surface, and the residues composing the pockets were well conserved.
S. aureus
YabJ was highly stable after chlorination, and the chlorinated state is reversible by treatment with DTT. However, it shows no chaperone activity after chlorination. Instead, YabJ from
S. aureus
shows chlorination-induced
ribonuclease
activity, and the activity is diminished after subsequent reduction. Even though the
yabJ
genes from
Staphylococcus
and
Bacillus
are clustered with regulators that are expected to code nucleic acid-interacting proteins, the nucleic acid-related activity of bacterial RidA has not been identified before. From our study, we revealed the structure and function of
S. aureus
YabJ as a novel chlorination-activated
ribonuclease
. The present study will contribute to an in-depth understanding of chlorination as a PTM.
...
PMID:A novel chlorination-induced ribonuclease YabJ from
Staphylococcus aureus
. 3020 92
N
6
-Methyladenosine (m
6
A), the most prevalent internal modification associated with eukaryotic mRNAs, influences many steps of mRNA metabolism, including splicing, export, and translation, as well as stability. Recent studies have revealed that m
6
A-containing mRNAs undergo one of two distinct pathways of rapid degradation: deadenylation via the YT521-B homology (YTH) domain-containing family protein 2 (YTHDF2; an m
6
A reader protein)-CCR4/NOT (deadenylase) complex or endoribonucleolytic cleavage by the YTHDF2-
HRSP12
-
ribonuclease
(
RNase
) P/mitochondrial RNA-processing (MRP) (endoribonuclease) complex. Some m
6
A-containing circular RNAs (circRNAs) are also subject to endoribonucleolytic cleavage by YTHDF2-
HRSP12
-RNase P/MRP. Here, we highlight recent progress on the molecular mechanisms underlying rapid mRNA degradation via m
6
A and describe our current understanding of the dynamic regulation of m
6
A-mediated mRNA decay through the crosstalk between m
6
A (or YTHDF2) and other cellular factors.
...
PMID:Molecular Mechanisms Driving mRNA Degradation by m
6
A Modification. 3196 9
