Reference "Cloning and characterization of several cDNAs for UDP-glucose pyrophosphorylase from barley (Hordeum vulgare) tissues"

Reference ID

8760

Title

Cloning and characterization of several cDNAs for UDP-glucose pyrophosphorylase from barley (Hordeum vulgare) tissues

Source

Gene, 1996, vol. 170, pp. 227-232

Authors (4)

Eimert-K	Villand-P
Kilian-A	Kleczkowski-L-A

Abstract

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.