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:3.1.26.5 (
RNase P
)
1,348
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
We have identified the functional promoter of the translational inhibitor p14.5, the human homologue to a rat perchloric acid-soluble protein (PSP), a mouse heat-responsive protein (Hrp12) and a goat tumor antigen (
UK114
). Sequence analysis revealed a GC-rich promoter with several consensus sequences for transcription factors, but no TATA- and CAAT-box. To confirm promoter activity, DNA fragments of the p14.5 5'-flanking region were ligated in front of the luciferase gene and were transfected into HeLa and HepG2 cells. A minimal promoter between nt -104 and nt +88 relative to the transcription start site was responsible for basal activity. Furthermore, we observed a head-to-head orientation of p14.5 to the gene for the protein subunit of
RNase P
and MRP ribonucleoproteins (hPOP1). Luciferase assays with fragments of the hPOP1 5'-flanking region revealed a minimal promoter between nt -20 and nt +98 relative to the start of transcription. These data indicate that the 102 bp region between p14.5 and hPOP1 can act as a bidirectional promoter. The p14.5-hPOP1-cluster was mapped to chromosome 8q22 using in situ hybridization technique.
...
PMID:A bidirectional promoter connects the p14.5 gene to the gene for RNase P and RNase MRP protein subunit hPOP1. 940 34
N
6
-methyladenosine (m
6
A) is the most abundant internal modification in RNAs and plays regulatory roles in a variety of biological and physiological processes. Despite its important roles, the molecular mechanism underlying m
6
A-mediated gene regulation is poorly understood. Here, we show that m
6
A-containing RNAs are subject to endoribonucleolytic cleavage via YTHDF2 (m
6
A reader protein),
HRSP12
(adaptor protein), and
RNase P
/MRP (endoribonucleases). We demonstrate that
HRSP12
functions as an adaptor to bridge YTHDF2 and
RNase P
/MRP, eliciting rapid degradation of YTHDF2-bound RNAs. Transcriptome-wide analyses show that m
6
A RNAs that are preferentially targeted for endoribonucleolytic cleavage have an
HRSP12
-binding site and a
RNase P
/MRP-directed cleavage site upstream and downstream of the YTHDF2-binding site, respectively. We also find that a subset of m
6
A-containing circular RNAs associates with YTHDF2 in an
HRSP12
-dependent manner and is selectively downregulated by
RNase P
/MRP. Thus, our data expand the known functions of
RNase P
/MRP to endoribonucleolytic cleavage of m
6
A RNAs.
...
PMID:Endoribonucleolytic Cleavage of m
6
A-Containing RNAs by RNase P/MRP Complex. 3093 54
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
