Identification and characterization of RED120: a conserved PWI domain protein with links to splicing and 3'-end formation

Puri Fortes, Dasa Longman, Susan McCracken, Joanna Y Ip, Raymond Poot, Iain W Mattaj, Javier F Cáceres, Benjamin J Blencowe

Research output: Contribution to journalArticlepeer-review

Abstract

Precursor (pre)-mRNA splicing can impact the efficiency of coupled steps in gene expression. SRm160 (SR-related nuclear matrix protein of 160 kDa), is a splicing coactivator that also functions as a 3'-end cleavage-stimulatory factor. Here, we have identified an evolutionary-conserved SRm160-interacting protein, referred to as hRED120 (for human Arg/Glu/Asp-rich protein of 120 kDa). hRED120 contains a conventional RNA recognition motif and, like SRm160, a PWI nucleic acid binding domain, suggesting that it has the potential to bridge different RNP complexes. Also, similar to SRm160, hRED120 associates with snRNP components, and remains associated with mRNA after splicing. Simultaneous suppression in Caenorhabditis elegans of the ortholog of hRED120 with the orthologs of splicing and 3'-end processing factors results in aberrant growth or developmental defects. These results suggest that RED120 may function to couple splicing with mRNA 3'-end formation.
Original languageEnglish
Pages (from-to)3087-97
Number of pages11
JournalFEBS Letters
Volume581
Issue number16
DOIs
Publication statusPublished - 26 Jun 2007

Keywords

  • Amino Acid Sequence
  • Animals
  • Antigens, Nuclear
  • Caenorhabditis elegans
  • Cell Nucleus
  • Cloning, Molecular
  • Conserved Sequence
  • HeLa Cells
  • Humans
  • Molecular Sequence Data
  • Nuclear Matrix-Associated Proteins
  • Phylogeny
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA 3' End Processing
  • RNA Precursors
  • RNA Splicing
  • RNA, Messenger
  • RNA-Binding Proteins
  • Sequence Homology, Amino Acid

Fingerprint

Dive into the research topics of 'Identification and characterization of RED120: a conserved PWI domain protein with links to splicing and 3'-end formation'. Together they form a unique fingerprint.

Cite this