Characterization of rps17, rpl9 and rpl15: three nucleus-encoded plastid ribosomal protein genes

Michael D. Thompson, Colleen M. Jacks, Todd R. Lenvik, J. Stephen Gantt

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26 Scopus citations

Abstract

Approximately two-thirds of the 55 to 60 plastid ribosomal proteins are encoded in the nucleus. Since the protein products of each of these genes are needed in equal amounts for ribosome assembly, their expression may be coordinately regulated by common mechanisms. To begin to understand how the expression of these genes is regulated, we have isolated cDNA and genomic clones for three plastid ribosomal protein genes from an Arabidopsis thaliana library. The genes rps17, rpl9 and rpl15, encoding plastid ribosomal proteins CS17, CL9 and CL15, respectively, are located in the nuclear genome and Southern blot data suggest that each is a single copy gene in A. thaliana. Northern blot data show that transcripts from rps17, rpl9 and rpl15 are much more abundant in leaves and stems than they are in roots. The nucleotide sequences of each of these three genes were determined and their transcriptional initiation sites identified. rps17 transcripts have multiple 5′ ends suggesting that they are initiated at multiple sites or are post-transcriptionally processed at their 5′ end. rpl9 and rpl15 apparently have unique transcriptional initiation sites but are post-transcriptionally processed to remove six and three introns, respectively, from their primary transcripts. We have examined the genomic sequences for motifs that may be important for the proper expression of these genes. A 7 bp sequence motif, whose consensus is 5′-AGGCCCA-3′, flanked by AT-rich regions was identified between 38 and 73 nucleotides upstream of the rps17, rpl9 and rpl15 transcriptional initiation sites.

Original languageEnglish (US)
Pages (from-to)931-944
Number of pages14
JournalPlant molecular biology
Volume18
Issue number5
DOIs
StatePublished - Mar 1 1992

Keywords

  • Arabidopsis thaliana
  • chloroplast
  • differential gene expression
  • gene structure
  • ribosomal protein

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