The Arabidopsis thaliana putative sialyltransferase resides in the Golgi apparatus but lacks the ability to transfer sialic acid

S. M. Daskalova, A. R. Pah, D. P. Baluch, L. C. Lopez

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

A common feature of the animal sialyltransferases (STs) is the presence of four conserved motifs, namely large (L), small (S), very small (VS) and motif III. Although sialic acid (SA) has not been detected in plants, three orthologues containing sequences similar to the ST motifs have been identified in the Arabidopsis thaliana L. database. In this study, we report that the gene (Gene ID: 824043) codes for a Golgi resident protein lacking the ability to transfer SA to asialofetuin or Galβ1,3GalNAc and Galβ1,4GlcNAc oligosaccharide acceptors. Restoration of deteriorated motifs S, VS and motif III by constructing chimeric proteins consisting of the 28-308 amino acid region of the A. thaliana ST-like protein and the 264-393 amino acid region of the Oryza sativa L. ST-like protein, or of the 28-240 amino acid region of the protein and the 204-350 amino acid region of the Homo sapiens L. α2,3-ST () was not able to recover sialyltransferase activity. Altering the appropriate amino acid regions of the A. thaliana ST-like protein to those typical for the mammalian motif III (HHYWE) and VS motif (HDADFE) also did not have any effect. Our data, together with previous results, indicate that A. thaliana in particular, and plants in general, do not have transferases for SA. Substrates for the plant ST-like proteins might be compounds involved in secondary metabolism.

Original languageEnglish (US)
Pages (from-to)284-299
Number of pages16
JournalPlant Biology
Volume11
Issue number3
DOIs
StatePublished - May 1 2009

Keywords

  • Arabidopsis
  • Chimeric protein
  • Sialyltransferase

ASJC Scopus subject areas

  • Ecology, Evolution, Behavior and Systematics
  • Plant Science

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