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

✍ Scribed by M. Dolors Ludevid; Miguel Angel Freire; Jordi Gómez; Christopher G. Burd; Fernando Albericio; Ernest Giralt; Gideon Dreyfuss; Montserrat Pagès

• Publisher: John Wiley and Sons
• Year: 1992
• Tongue: English
• Weight: 468 KB
• Volume: 2
• Category: Article
• ISSN: 0960-7412
• DOI: 10.1046/j.1365-313x.1992.t01-10-00999.x

✦ Synopsis

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.