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Alternative splicing results in two different transcripts for H‐protein of the glycine cleavage system in the C 4 species Flaveria trinervia
Author(s) -
Kopriva Stanislav,
Cossu Roberto,
Bauwe Hermann
Publication year - 1995
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.1995.08030435.x
Subject(s) - alternative splicing , biology , exon , gene , glycine cleavage system , rna splicing , intron , complementary dna , genetics , coding region , messenger rna , microbiology and biotechnology , glycine , rna , amino acid
Alternative splicing is a well‐known post‐transcriptional regulatory mechanism in eukaryotic organisms but there are only very few reports on alternative splicing in plants. The analysis of cDNAs encoding H‐protein of the glycine decarboxylase multi‐enzyme complex from the C 4 species Flaveria trinervia revealed the presence of two transcript populations that differ in the length of their coding regions by six nucleotides. Otherwise, including their 3′ non‐translated region, they are identical. From a genomic Southern analysis and from the sequencing of several independent cDNA clones it is evident that both types of transcript are derived from a single‐copy gene. This gene, FT gdcsH , has been cloned and sequenced. It comprises four short exons. The two alternative splice sites are located at the end of intron 1. The shorter transcript closely corresponds to published H‐protein mRNA sequences from other organisms. The longer transcript encodes two additional alanine residues very close to the N‐terminus of the mature H‐protein. A quantification of the relative amounts of both transcripts in different organs revealed that, with 80–90% of the total H‐protein mRNA, the alternative mRNA dominates in leaves whereas roots contain more of the ‘correctly’ spliced transcript. It is concluded that, in F. trinervia and with a distinct organ preference, alternative splicing leads to the synthesis of two different H‐proteins of the glycine cleavage system.

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