Nucleic Acids Research, Vol 26, Issue 10 2265-2272, Copyright © 1998 by Oxford University Press
C Alexander, N Faber and P Klaff
RNA-binding proteins play a major role in regulating mRNA metabolism in
chloroplasts. In this work we characterized two proteins, of 43 and 47 kDa,
which bind to the spinach psbA mRNA 5' untranslated region (psbA encoding
the D1 protein of photosystem II). The 43 kDa protein, which is present in
the stroma and in membranes, co-sediments with a complex of 68S. It was
purified, and the N-terminal sequence was determined. Upon homology search
it was identified as the chloroplast homologue of the Escherichia coli
ribosomal protein S1. The 47 kDa protein, which, in contrast with the 43
kDa protein, sediments with a small sedimentation coefficient, is only
detected in the stromal fraction. It is soluble in an uncomplexed form. By
deletion analysis, an element within the psbA mRNA 5' untranslated region
was identified that is necessary but not sufficient for binding of stromal
proteins. The 'central protein binding element' ranges from nucleotide -49
to -9 of the psbA mRNA 5' untranslated region. It comprises the
Shine-Dalgarno- like GGAG motif and, 7 nucleotides upstream, an
endonucleolytic cleavage site involved in psbA mRNA degradation in vitro .
The mechanistic impacts of this region in relation to RNA-binding proteins
are discussed.
ARTICLES
Characterization of protein-binding to the spinach chloroplast psbA mRNA 5' untranslated region
Institut fur Physikalische Biologie, Heinrich-Heine-Universitat Dusseldorf, Universitatsstrasse 1, D-40225 Dusseldorf, Germany.
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