Molecular Cloning of Pigeon UDP-galactose:β-d-Galactoside α1,4-Galactosyltransferase and UDP-galactose:β-d-Galactoside β1,4-Galactosyltransferase, Two Novel Enzymes Catalyzing the Formation of Galα1–4Galβ1–4Galβ1–4GlcNAc Sequence

Suzuki, Noriko; Yamamoto, Kazuo

doi:10.1074/jbc.m109.018663

Cited by 24 publications

(33 citation statements)

References 48 publications

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“…Since both species belong to Neoaves, Galβ1-4Gal seems to be expressed in some other birds belonging to Neoaves. The expression of Galβ1-4Gal in Neoaves is supported by the fact that another Neoaves, zebra finch, possesses a gene which is similar to pigeon β4GalT(Gal) cDNA [36]. In addition, we found that Galβ1-4Gal on glycoproteins is also expressed in ostrich, which belongs to Ratitae [15].…”

Section: Discussionmentioning

confidence: 58%

Distribution of the Galβ1-4Gal Epitope among Birds: Species-Specific Loss of the Glycan Structure in Chicken and Its Relatives

Suzuki

Nawa

et al. 2013

PLoS ONE

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The Galβ1-4Gal epitope is rarely found in mammals, and the natural antibody against Galβ1-4Gal is rich in human. In contrast, we have previously demonstrated the presence of Galβ1-4Gal in pigeon and ostrich, and the absence of this epitope in chicken. Here, to further investigate the expression of this glycan among birds, egg white glycoproteins and egg yolk IgG from nine species of birds, namely, chicken, duck, emu, guineafowl, ostrich, peafowl, pigeon, quail, and turkey, were analyzed by western blot using an anti-(Galβ1-4Gal) antibody. The results indicated that some egg white glycoproteins from emu, ostrich, and quail, and heavy chains of IgG from all of the birds, except chicken and quail, were stained with the antibody. The presence of Galβ1-4Gal on N-glycans of IgGs from guineafowl, peafowl, and turkey were confirmed by mass spectrometry (MS), MS/MS, and MSn analyses. In quail, the presence of Galβ1-4Gal was confirmed by detecting the activities of UDP-galactose: β-galactoside β1,4-galactosyltransferase (β4GalT(Gal)) in various tissues, and by detecting Galβ1-4Gal by western blotting. In contrast, bamboo partridge, which is a close relative of chicken, did not show any detectable activities of β4GalT(Gal) or Galβ1-4Gal on glycoproteins. Because quail, peafowl, turkey, chicken, and bamboo partridge belong to the same family, i.e., Phasianidae, expression of Galβ1-4Gal was most likely differentiated within this family. Considering that Galβ1-4Gal is also expressed in ostrich, emu, and pigeon, which are phylogenetically distant relatives within modern birds, Galβ1-4Gal expression appears to be widely distributed among birds, but might have been abolished in the ancestors of chicken and bamboo partridge.

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Section: Discussionmentioning

confidence: 58%

Distribution of the Galβ1-4Gal Epitope among Birds: Species-Specific Loss of the Glycan Structure in Chicken and Its Relatives

Suzuki

Nawa

et al. 2013

PLoS ONE

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“…The 3 long-standing hypotheses about the genetic relationship between the P1 and P k antigens outlined in the introduction can now be evaluated in a new light. As indicated by our discovery of a P 1 /P 2 -predictive SNP in the novel exon 2a of A4GALT and also suggested by previous studies, 32,36 it is highly likely that the ␣4GalT encoded by A4GALT, synthesizes both antigens. Accordingly, the concept of a closely linked homologous galactosyltransferase gene, 30 which encodes for P1 synthesis only while the A4GALT product makes P k , can be ruled out.…”

Section: Discussionmentioning

confidence: 75%

“…35 It was recently reported that the human and chicken ␣4Gal-T enzymes can synthesize P k and P1 glycolipids in an in vitro transfection model, whereas the pigeon counterpart makes only P1 antigen on glycoproteins. 36 The glycoconjugates produced were not fully characterized but nevertheless this study again focused attention on A4GALT. We therefore set out to elucidate the genetic basis of the P 1 /P 2 phenotypes and found transcripts with a novel A4GALT exon containing 3 polymorphic nucleotides, one of which predicts the presence of P1 antigen.…”

Section: Introductionmentioning

confidence: 99%

Identification of a novel A4GALT exon reveals the genetic basis of the P1/P2 histo-blood groups

Thuresson

Westman

Olsson

2011

Blood

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The A4GALT locus encodes a glycosyltransferase that synthesizes the terminal Gal␣1-4Gal of the P k (Gb3/CD77) glycosphingolipid, important in transfusion medicine, obstetrics, and pathogen susceptibility. Critical nucleotide changes in A4GALT not only abolish P k formation but also another Gal␣1-4Gal-defined antigen, P1, which belongs to the only blood group system for which the responsible locus remains undefined. Since known A4GALT polymorphisms do not explain the P1؊P k ؉ phenotype, P 2 , we set out to elucidate the genetic basis of P 1 /P 2 . Despite marked differences (P 1 > P 2 ) in A4GALT transcript levels in blood, luciferase experiments showed no difference between P 1 /P 2 -related promoter sequences. Investigation of A4GALT mRNA in cultured human bone marrow cells revealed novel transcripts containing only the noncoding exon 1 and a sequence (here termed exon 2a) from intron 1. These 5-capped transcripts include poly-A tails and 3 polymorphic sites, one of which was P 1 /P 2 -specific among > 200 donors and opens a short reading frame in P 2 alleles. We exploited these data to devise the first genotyping assays to predict P1 status. P 1 /P 2 genotypes correlated with both transcript levels and P1/P k expression on red cells. Thus, P 1 zygosity partially explains the well-known interindividual variation in P1 strength. Future investigations need to focus on regulatory mechanisms underlying P1 synthesis. (Blood. 2011; 117(2):678-687)

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“…Recently, a new family of glycosyltransferases, GT92, was added to CAZy with the identification of novel b-1,4-galactosyltransferases in animals. The GT92 proteins are reported from pigeon (Columba livia), where they catalyze the transfer of b-1,4-linked Gal onto b-1,4-linked Gal in N-glycan structures (Suzuki and Yamamoto, 2010). However, genes encoding GT92 proteins are not found in all birds or in mammals.…”

Section: Glycosyltransferase Family Gt92 Contains B-14-galactosyltramentioning

confidence: 99%

Pectin Biosynthesis: GALS1 in Arabidopsis thaliana Is a β-1,4-Galactan β-1,4-Galactosyltransferase

et al. 2012

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b-1,4-Galactans are abundant polysaccharides in plant cell walls, which are generally found as side chains of rhamnogalacturonan I. Rhamnogalacturonan I is a major component of pectin with a backbone of alternating rhamnose and galacturonic acid residues and side chains that include a-1,5-arabinans, b-1,4-galactans, and arabinogalactans. Many enzymes are required to synthesize pectin, but few have been identified. Pectin is most abundant in primary walls of expanding cells, but b-1,4-galactan is relatively abundant in secondary walls, especially in tension wood that forms in response to mechanical stress. We investigated enzymes in glycosyltransferase family GT92, which has three members in Arabidopsis thaliana, which we designated GALACTAN SYNTHASE1, (GALS1), GALS2 and GALS3. Loss-of-function mutants in the corresponding genes had a decreased b-1,4-galactan content, and overexpression of GALS1 resulted in plants with 50% higher b-1,4-galactan content. The plants did not have an obvious growth phenotype. Heterologously expressed and affinity-purified GALS1 could transfer Gal residues from UDP-Gal onto b-1,4-galactopentaose. GALS1 specifically formed b-1,4-galactosyl linkages and could add successive b-1,4-galactosyl residues to the acceptor. These observations confirm the identity of the GT92 enzyme as b-1,4-galactan synthase. The identification of this enzyme could provide an important tool for engineering plants with improved bioenergy properties.

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Molecular Cloning of Pigeon UDP-galactose:β-d-Galactoside α1,4-Galactosyltransferase and UDP-galactose:β-d-Galactoside β1,4-Galactosyltransferase, Two Novel Enzymes Catalyzing the Formation of Galα1–4Galβ1–4Galβ1–4GlcNAc Sequence

Cited by 24 publications

References 48 publications

Distribution of the Galβ1-4Gal Epitope among Birds: Species-Specific Loss of the Glycan Structure in Chicken and Its Relatives

Distribution of the Galβ1-4Gal Epitope among Birds: Species-Specific Loss of the Glycan Structure in Chicken and Its Relatives

Identification of a novel A4GALT exon reveals the genetic basis of the P1/P2 histo-blood groups

Pectin Biosynthesis: GALS1 in Arabidopsis thaliana Is a β-1,4-Galactan β-1,4-Galactosyltransferase

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