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Cloning and characterization of several cDNAs for UDP-glucose pyrophosphorylase from barley (Hordeum vulgare) tissues
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC). (Leszek Kleczkowski)ORCID iD: 0000-0001-8685-9665
1996 (English)In: Gene, ISSN 0378-1119, E-ISSN 1879-0038, Vol. 170, no 2, 227-232 p.Article in journal (Refereed) Published
Abstract [en]

Eleven cDNA clones encoding UDP-glucose pyrophosphorylase (UGPase) have been isolated from cDNA libraries prepared from seed embryo, seed endosperm and leaves of barley (Hordeum vulgare L.). The sequences were identical, with the exception of positioning of the poly(A) tail; at least five clones with different polyadenylation sites were found. For a putative full-length cDNA [1775 nucleotides (nt) plus polyadenylation tail], isolated from an embryo cDNA library, an open reading frame of 1419 nt encodes a protein of 473 amino acids (aa) of 51.6 kDa. An alignment of the derived aa sequence with other UGPases has revealed high identity to UGPases from eukaryotic tissues, but not from bacteria. Within the aa sequence, no homology was found to a UDP-glucose-binding motif that has been postulated for a family of glucosyl transferases. The derived aa sequence of UGPase contains three putative N-glycosylation sites and has a highly conserved positioning of five Lys residues, previously shown to be critical for catalysis and substrate binding of potato tuber UGPase. A possible role for N-glycosylation in the intracellular targeting of UGPase is discussed.

Place, publisher, year, edition, pages
1996. Vol. 170, no 2, 227-232 p.
Keyword [en]
ADP-glucose pyrophosphorylase, cytosol, N-glycosylation, polyadenylation, starch, sucrose, UDP-glucose binding site
URN: urn:nbn:se:umu:diva-44751ISI: A1996UL65800012OAI: diva2:424379
Available from: 2011-06-17 Created: 2011-06-09 Last updated: 2015-04-29

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