Galectin-3 is a nuclear matrix protein which binds RNA

Li Wang, Hidenori Inohara, Kenneth J. Pienta, Avraham Raz

Research output: Contribution to journalArticlepeer-review

Abstract

The endogenous galectin-3 is a carbohydrate-binding protein of Mr∼30,000 serving in the cytoplasm and on the cell surface as a receptor for ligands containing poly-N-acetyllactosamine sequences. In addition, galectin-3 has been demonstrated to be associated in the nucleus with ribonucleoprotein complexes and to act as a pre-mRNA splicing factor and to be involved in spliceosome assembly. However, little is known about either its nuclear localization or its ligand(s), respectively. We demonstrate directly here that galectin-3 is associated with the RNA protein skeleton of the nucleus, i.e., the nuclear matrix, and binds with single-stranded DNA (ssDNA) and with RNA. The affinity of binding was determined to be 2.3 μM. Lactose, which inhibits galectin-3 binding to glycoconjugates, failed to inhibit either galectin-3-ssDNA or galectin-3-RNA binding. Galectin-3 exhibited the highest affinity to poly(A) ribonucleotide homopolymers. The results presented here shows that galectin-3 may act as a RNA-binding protein in the nuclear matrix in a noncarbohydrate-dependent manner.

Original languageEnglish (US)
Pages (from-to)292-303
Number of pages12
JournalBiochemical and Biophysical Research Communications
Volume217
Issue number1
DOIs
StatePublished - Jan 1 1995
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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