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

Functional Cus1p is found with Hsh155p in a multiprotein splicing factor associated with U2 snRNA.

Molecular and cellular biology - 1 Mar 2000

Pauling M H, McPheeters D S, Ares M

Abstract excerpt

To explore the dynamics of snRNP structure and function, we have studied Cus1p, identified as a suppressor of U2 snRNA mutations in budding yeast. Cus1p is homologous to human SAP145, a protein present in the 17S form of the human U2 snRNP. Here, we define the Cus1p amino acids required for function in yeast. The segment of Cus1p required for binding to Hsh49p, a homolog of human SAP49, is contained within an...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Signal Transducing
Share to Phosphoproteins
Share to Ribonucleoprotein, U2 Small Nuclear

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ribosomal Proteins

Share to RNA-Binding Proteins

Share to RNA, Small Nuclear

Share to RNA Splicing

Share to RNA Splicing Factors

Source

Open in PubMed Open full text

Identifiers

PMID: 10688664
DOI: 10.1128/MCB.20.6.2176-2185.2000
PMCID: PMC110834

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional Cus1p is found with Hsh155p in a multiprotein splicing factor associated with U2 snRNA.PMID 10688664Read ↗

Cus2 enforces the first ATP-dependent step of splicing by binding to yeast SF3b1 through a UHM-ULM interactionSemantic proximity Read ↗

A comprehensive biochemical and genetic analysis of the yeast U1 snRNP reveals five novel proteins.Semantic proximity Read ↗

Structure-function analysis of the Yhc1 subunit of yeast U1 snRNP and genetic interactions of Yhc1 with Mud2, Nam8, Mud1, Tgs1, U1 snRNA, SmD3 and Prp28.Semantic proximity Read ↗

SF3B1/Hsh155 HEAT motif mutations affect interaction with the spliceosomal ATPase Prp5, resulting in altered branch site selectivity in pre-mRNA splicing.Semantic proximity Read ↗

Rds3p is required for stable U2 snRNP recruitment to the splicing apparatus.Semantic proximity Read ↗

Partial purification of the yeast U2 snRNP reveals a novel yeast pre-mRNA splicing factor required for pre-spliceosome assembly.Semantic proximity Read ↗

Functional analysis of Hsh155/SF3b1 interactions with the U2 snRNA/branch site duplex.Semantic proximity Read ↗

An intronic RNA structure modulates expression of the mRNA biogenesis factor Sus1.Semantic proximity Read ↗

Characterization of yeast U1 snRNP A protein: identification of the N-terminal RNA binding domain (RBD) binding site and evidence that the C-terminal RBD functions in splicing.Semantic proximity Read ↗

Structure-function analysis of the 5' end of yeast U1 snRNA highlights genetic interactions with the Msl5*Mud2 branchpoint-binding complex and other spliceosome assembly factors.Semantic proximity Read ↗

Cloning of a yeast U1 snRNP 70K protein homologue: functional conservation of an RNA-binding domain between humans and yeast.Semantic proximity Read ↗

Structure-function analysis and genetic interactions of the Luc7 subunit of the Saccharomyces cerevisiae U1 snRNP.Semantic proximity Read ↗

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