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

LUDEVID MD, FREIRE MA, GÓMEZ J, BURD CG, ALBERICIO F, GIRALT E, DREYFUSS G, PAGÈS M

PLANT JOURNAL

Blackwell

Año: 1992 vol. 2 p. 999 - 1003

0960-7412

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.