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

Stem-loop binding protein facilitates 3'-end formation by stabilizing U7 snRNP binding to histone pre-mRNA.

Molecular and cellular biology - 1 May 1999

Dominski Z, Zheng L X, Sanchez R, Marzluff W F

Abstract excerpt

The 3' end of histone mRNA is formed by an endonucleolytic cleavage of the primary transcript after a conserved stem-loop sequence. The cleavage reaction requires at least two trans-acting factors: the stem-loop binding protein (SLBP), which binds the stem-loop sequence, and the U7 snRNP that interacts with a sequence downstream from the cleavage site. Removal of SLBP from a nuclear extract abolishes 3'-end...

Read the complete abstract on PubMed

Topics

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

Share to Histones
Share to mRNA Cleavage and Polyadenylation Factors

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Nucleic Acid Conformation

Share to Ribonucleoproteins, Small Nuclear

Share to RNA-Binding Proteins

Share to RNA Precursors

Share to RNA Processing, Post-Transcriptional

Share to Sequence Deletion

Source

Open in PubMed Open full text

Identifiers

PMID: 10207079
DOI: 10.1128/MCB.19.5.3561
PMCID: PMC84148

Genes

SLBP

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Stem-loop binding protein facilitates 3'-end formation by stabilizing U7 snRNP binding to histone pre-mRNA.PMID 10207079Read ↗

Mutations in the RNA binding domain of stem-loop binding protein define separable requirements for RNA binding and for histone pre-mRNA processing.Semantic proximity Read ↗

U7 snRNP is recruited to histone pre-mRNA in a FLASH-dependent manner by two separate regions of the stem-loop binding protein.Semantic proximity Read ↗

Changes in the stem-loop at the 3' terminus of histone mRNA affects its nucleocytoplasmic transport and cytoplasmic regulation.Semantic proximity Read ↗

Differences and similarities between Drosophila and mammalian 3' end processing of histone pre-mRNAs.Semantic proximity Read ↗

The 68 kDa subunit of mammalian cleavage factor I interacts with the U7 small nuclear ribonucleoprotein and participates in 3'-end processing of animal histone mRNAs.Semantic proximity Read ↗

Functional importance of conserved nucleotides at the histone RNA 3' processing site.Semantic proximity Read ↗

The N-terminal domains of FLASH and Lsm11 form a 2:1 heterotrimer for histone pre-mRNA 3'-end processing.Semantic proximity Read ↗

3' end mRNA processing: molecular mechanisms and implications for health and disease.Semantic proximity Read ↗

Loss of the histone pre-mRNA processing factor stem-loop binding protein in Drosophila causes genomic instability and impaired cellular proliferation.Semantic proximity Read ↗

Drosophila stem loop binding protein coordinates accumulation of mature histone mRNA with cell cycle progression.Semantic proximity Read ↗

Structure of the histone mRNA hairpin required for cell cycle regulation of histone gene expression.Semantic proximity Read ↗

SMN Is Essential for the Biogenesis of U7 Small Nuclear Ribonucleoprotein and 3′-End Formation of Histone mRNAsSemantic proximity Read ↗

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