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RNA binding characteristics of a 16 kDa glycine‐rich protein from maize
Author(s) -
Ludevid M. Dolors,
Freire Miguel Angel,
Gómez Jordi,
Burd Christopher G.,
Albericio Fernando,
Giralt Ernest,
Dreyfuss Gideon,
Pagès Montserrat
Publication year - 1992
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1992.t01-10-00999.x
Subject(s) - rna binding protein , rna , ribonucleoprotein , biology , biochemistry , messenger rnp , binding protein , messenger rna , microbiology and biotechnology , binding site , gene
Summary 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 (MA 16) 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.