Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Protein-protein and protein-RNA contacts both contribute to the 15.5K-mediated assembly of the U4/U6 snRNP and the box C/D snoRNPs.

Molecular and cellular biology - 1 Jul 2006

Schultz Annemarie, Nottrott Stephanie, Watkins Nicholas James, Lührmann Reinhard

Abstract excerpt

The k-turn-binding protein 15.5K is unique in that it is essential for the hierarchical assembly of three RNP complexes distinct in both composition and function, namely, the U4/U6 snRNP, the box C/D snoRNP, and the RNP complex assembled on the U3 box B/C motif. 15.5K interacts with the cognate R...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Conserved Sequence
Share to Nucleic Acid Conformation
Share to Protein Interaction Mapping

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ribonucleoprotein, U4-U6 Small Nuclear

Share to Ribonucleoproteins, Small Nuclear

Share to Ribonucleoproteins, Small Nucleolar

Share to RNA, Small Nucleolar

Source

Open in PubMed Open full text

Identifiers

PMID: 16782898
DOI: 10.1128/MCB.02374-05
PMCID: PMC1489164

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-16782898-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Protein-protein and protein-RNA contacts both contribute to the 15.5K-mediated assembly of the U4/U6 snRNP and the box C/D snoRNPs.PMID 16782898Read ↗

A structural, phylogenetic, and functional study of 15.5-kD/Snu13 protein binding on U3 small nucleolar RNA.Semantic proximity Read ↗

Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP.Semantic proximity Read ↗

Analysis of Snu13p mutations reveals differential interactions with the U4 snRNA and U3 snoRNA.Semantic proximity Read ↗

Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP protein with the 5' stem-loop of U4 snRNA.Semantic proximity Read ↗

Reconstitution of the human U snRNP assembly machinery reveals stepwise Sm protein organization.Semantic proximity Read ↗

Structural basis for recognition of intron branchpoint RNA by yeast Msl5 and selective effects of interfacial mutations on splicing of yeast pre-mRNAs.Semantic proximity Read ↗

The SBP2 and 15.5 kD/Snu13p proteins share the same RNA binding domain: identification of SBP2 amino acids important to SECIS RNA binding.Semantic proximity Read ↗

Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP.Semantic proximity Read ↗

Structure-function analysis and genetic interactions of the yeast branchpoint binding protein Msl5.Semantic proximity Read ↗

The network of protein–protein interactions within the human U4/U6.U5 tri-snRNPSemantic proximity Read ↗

The U5 snRNA internal loop 1 is a platform for Brr2, Snu114 and Prp8 protein binding during U5 snRNP assembly.Semantic proximity Read ↗

Role of conserved nucleotides in building the 16 S rRNA binding site for ribosomal protein S15.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.