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

1992; Wiley; Volume: 2; Issue: 6 Linguagem: Inglês

10.1046/j.1365-313x.1992.t01-10-00999.x

1365-313X

M. Dolors Ludevid, Miguel Ángel Freire, Jordi Gómez, Christopher G. Burd, Fernando Alberício, Ernest Giralt, Gideon Dreyfuss, Montserrat Pagès,

Plant Genetic and Mutation Studies

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.