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Plant Mol Biol. 1996 Mar;30(6):1195-205.

RNA-binding proteins of 37/38 kDa bind specifically to the barley chloroplast psbA 3'-end untranslated RNA.

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Department of Biochemistry and Biophysics, Texas A & M University, College Station 77843, USA.


The stability of the psbA mRNA increases during barley chloroplast development eventually reaching a half-life of over 40 h. Translation of psbA mRNA is also regulated in a complex way. Sequence-specific RNA binding proteins may modulate the translation or stability of the psbA mRNA during chloroplast development. UV cross-linking assays revealed that chloroplast proteins of 37 and 38 kDA bind specifically to the 3' end of psbA transcripts and not to the 5' end of psbA or rbcL transcripts. The two RNA-binding proteins were partially purified by ammonium sulfate precipitation followed by heparin agarose chromatography. Deletion and site-directed mutation analysis demonstrated that the 37/38RNPs bind in a 30 nucleotide region immediately downstream from the translation termination codon and upstream of sequences capable of forming a stem-loop structure in the 3' end of psbA transcripts. Single-base changes that diminish the binding of the 37RNP also reduce binding of the 38RNP suggesting that these proteins may bind as a heterodimer. The 37/38RNPs that bind within the 3' end of psbA transcripts could modulate transcription termination, translation or mRNA stability.

[Indexed for MEDLINE]

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