Binding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution.
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Signal recognition particle components in the nucleolusAlu elements as regulators of gene expressionPurification, characterization, and cloning of the cDNA of human signal recognition particle RNA 3'-adenylating enzymeHuman signal recognition particle (SRP) Alu-associated protein also binds Alu interspersed repeat sequence RNAs. Characterization of human SRP9A human Alu RNA-binding protein whose expression is associated with accumulation of small cytoplasmic Alu RNAStepwise RNP assembly at the site of H/ACA RNA transcription in human cellsStructure and assembly of the Alu domain of the mammalian signal recognition particleElongation arrest is a physiologically important function of signal recognition particle.Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression.The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure.Rapid nucleolytic degradation of the small cytoplasmic Y RNAs during apoptosisPost-transcriptional adenylation of signal recognition particle RNA is carried out by an enzyme different from mRNA Poly(A) polymeraseAlu RNP and Alu RNA regulate translation initiation in vitroA complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteinsMolecular evolution of SRP cycle components: functional implicationsA trinucleotide repeat-associated increase in the level of Alu RNA-binding protein occurred during the same period as the major Alu amplification that accompanied anthropoid evolutionLocalization of signal recognition particle RNA in the nucleolus of mammalian cellsNew insights into signal recognition and elongation arrest activities of the signal recognition particle.The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14.New prospects in studying the bacterial signal recognition particle pathway.Signal recognition particle (SRP), a ubiquitous initiator of protein translocation.Hierarchical assembly of the Alu domain of the mammalian signal recognition particle.The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAsThe 3' end formation in small RNAs.Crystal structure of a signal recognition particle Alu domain in the elongation arrest conformation.The SRP9/14 subunit of the human signal recognition particle binds to a variety of Alu-like RNAs and with higher affinity than its mouse homolog.A highly conserved nucleotide in the Alu domain of SRP RNA mediates translation arrest through high affinity binding to SRP9/14A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle.Alu transcripts: cytoplasmic localisation and regulation by DNA methylation.The heterodimeric subunit SRP9/14 of the signal recognition particle functions as permuted single polypeptide chainGenetic and biochemical analysis of the fission yeast ribonucleoprotein particle containing a homolog of Srp54p.The subset of mouse B1 (Alu-equivalent) sequences expressed as small processed cytoplasmic transcriptsReconstitution of human telomerase activity and identification of a minimal functional region of the human telomerase RNA.The decline in human Alu retroposition was accompanied by an asymmetric decrease in SRP9/14 binding to dimeric Alu RNA and increased expression of small cytoplasmic Alu RNA.Multiple dispersed loci produce small cytoplasmic Alu RNA.Periodic distribution of a putative nucleosome positioning motif in human, nonhuman primates, and archaea: mutual information analysisThe RNA polymerase III terminator used by a B1-Alu element can modulate 3' processing of the intermediate RNA productConserved 3' UTR stem-loop structure in L1 and Alu transposons in human genome: possible role in retrotransposition.Conserved tertiary base pairing ensures proper RNA folding and efficient assembly of the signal recognition particle Alu domain.Autoimmune diseases and polyamines.
P2860
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P2860
Binding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
Binding sites of the 9- and 14 ...... hat is conserved in evolution.
@ast
Binding sites of the 9- and 14 ...... hat is conserved in evolution.
@en
type
label
Binding sites of the 9- and 14 ...... hat is conserved in evolution.
@ast
Binding sites of the 9- and 14 ...... hat is conserved in evolution.
@en
prefLabel
Binding sites of the 9- and 14 ...... hat is conserved in evolution.
@ast
Binding sites of the 9- and 14 ...... hat is conserved in evolution.
@en
P2093
P2860
P356
P1476
Binding sites of the 9- and 14 ...... hat is conserved in evolution.
@en
P2093
P2860
P304
P356
10.1128/MCB.11.8.3949
P407
P577
1991-08-01T00:00:00Z