RNA binding characteristics of a 16 kDa glycine-rich protein from maize

Plant J. 1992 Nov;2(6):999-1003.

Abstract

We have previously described a developmentally regulated mRNA in maize that accumulates in mature embryos and is involved in a variety of stress responses in the plant. The sequence of the encoded 16 kDa protein (MA16) predicts that it is an RNA-binding protein, since it possesses a ribonucleoprotein consensus sequence-type RNA-binding domain (CS-RBD). To assess the predicted RNA binding property of the protein and as a starting point to characterize its function we have used ribohomopolymer-binding assays. Here we show that the MA16-encoded protein binds preferentially to uridine- and guanosine-rich RNAs. In light of these results a likely role for this protein in RNA metabolism during late embryogenesis and in the stress response is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Heat-Shock Proteins / genetics*
  • Heat-Shock Proteins / immunology
  • Heat-Shock Proteins / metabolism
  • Molecular Sequence Data
  • Plant Proteins / genetics*
  • Plant Proteins / immunology
  • Plant Proteins / metabolism
  • Poly A / metabolism
  • Poly C / metabolism
  • Poly G / metabolism
  • Poly U / metabolism
  • RNA-Binding Proteins / genetics*
  • RNA-Binding Proteins / metabolism
  • Seeds / metabolism
  • Zea mays / genetics*

Substances

  • Heat-Shock Proteins
  • Plant Proteins
  • RNA-Binding Proteins
  • GRP protein, Zea mays
  • Poly A
  • Poly G
  • Poly U
  • Poly C