Identification of the amino acid residue in the nematode galectin LEC-1 responsible for its unique sugar binding property: analysis by combination of site-directed mutagenesis and frontal affinity chromatography

• 資料種別: 記事
• タイトル: Identification of the amino acid residue in the nematode galectin LEC-1 responsible for its unique sugar binding property: analysis by combination of site-directed mutagenesis and frontal affinity chromatography
• 著者・編者: Yoichiro Arata; Norihide Ishii; Mayumi Tamura 他
• 著者標目: Yoichiro Arata; Norihide Ishii; Mayumi Tamura
• タイトル（掲載誌）: Biological and pharmaceutical bulletin
• 巻号年月日等（掲載誌）: 30(11) 2007.11
• 掲載巻: 30
• 掲載号: 11
• 掲載ページ: 2012～2017
• 掲載年月日（W3CDTF）: 2007-11
• ISSN（掲載誌）: 0918-6158
• ISSN-L（掲載誌）: 0918-6158
• 出版事項（掲載誌）: Tokyo : Pharmaceutical Society of Japan
• 出版地（国名コード）: JP
• 本文の言語コード: eng
• 件名標目: galectin; frontal affinity chromatography; site-directed mutagenesis; sugar-binding property; A-hexasaccharide; Caenorhabditis elegans
• NDLC: ZS51
• 対象利用者: 一般
• 所蔵機関: 国立国会図書館
• 請求記号: Z53-V41
• 連携機関・データベース: 国立国会図書館 : 国立国会図書館雑誌記事索引; https://ndlsearch.ndl.go.jp
• 書誌ID（NDLBibID）: 8965327; http://id.ndl.go.jp/bib/8965327
• 整理区分コード: 632

• 要約等: The basic disaccharide structure recognized by galectin family members is the lactosamine-like structure Galβ1-4(3)Glc(NAc). In galectins, eight highly conserved amino acid residues participate in the recognition of this basic structure. Each galectin seems to mediate diverse biological functions due to recognition of different modifications of the basic disaccharide Galβ1-4(3)Glc(NAc), but there is very little information about which amino acid residue in galectin is responsible for recognizing these modifications. The 32-kDa galectin LEC-1 of the nematode <i>Caenorhabditis elegans</i> is composed of two domains, each of which is homologous to vertebrate 14-kDa-type galectins. Although both lectin domains have an affinity for <i>N</i>-acetyllactosamine (Galβ1-4GlcNAc)-containing, <i>N</i>-linked, complex-type sugar chains, the N-terminal lectin domain of LEC-1 recognizes blood group A saccharide (GalNAcα1-3(Fucα1-2)Galβ1-3GlcNAc), whereas this saccharide is only poorly recognized by the C-terminal domain. Here, we used a combination of site-directed mutagenesis of the N-terminal lectin domain of galectin LEC-1 and an analysis of the sugar-binding profile by frontal affinity chromatography to identify the amino acid residues important for this recognition. Our results indicate that Thr⁴¹ in the N-terminal lectin domain of LEC-1 is important for its affinity for A-hexasaccharide.
• DOI: 10.1248/bpb.30.2012
• オンライン閲覧公開範囲: インターネット公開
• 連携機関・データベース: 科学技術振興機構 : J-STAGE; http://www.jstage.jst.go.jp

• 要約等: The basic disaccharide structure recognized by galectin family members is the lactosamine-like structure Galβ1-4(3)Glc(NAc). In galectins, eight highly conserved amino acid residues participate in the recognition of this basic structure. Each galectin seems to mediate diverse biological functions due to recognition of different modifications of the basic disaccharide Galβ1-4(3)Glc(NAc), but there is very little information about which amino acid residue in galectin is responsible for recognizing these modifications. The 32-kDa galectin LEC-1 of the nematode <i>Caenorhabditis elegans</i> is composed of two domains, each of which is homologous to vertebrate 14-kDa-type galectins. Although both lectin domains have an affinity for <i>N</i>-acetyllactosamine (Galβ1-4GlcNAc)-containing, <i>N</i>-linked, complex-type sugar chains, the N-terminal lectin domain of LEC-1 recognizes blood group A saccharide (GalNAcα1-3(Fucα1-2)Galβ1-3GlcNAc), whereas this saccharide is only poorly recognized by the C-terminal domain. Here, we used a combination of site-directed mutagenesis of the N-terminal lectin domain of galectin LEC-1 and an analysis of the sugar-binding profile by frontal affinity chromatography to identify the amino acid residues important for this recognition. Our results indicate that Thr⁴¹ in the N-terminal lectin domain of LEC-1 is important for its affinity for A-hexasaccharide.
• DOI: 10.1248/bpb.30.2012; https://doi.org/10.1248/bpb.30.2012
• オンライン閲覧公開範囲: インターネット公開
• 関連情報（URI）: http://id.ndl.go.jp/bib/8965327; https://ndlsearch.ndl.go.jp/books/R000000004-I8965327; http://www.jstage.jst.go.jp/article/bpb/30/11/30_11_2012/_pdf; https://teikyo-u.repo.nii.ac.jp/records/2060630; https://search.jamas.or.jp/link/ui/2008115424
• 参照: The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography; https://cir.nii.ac.jp/crid/1360567189460558464; S-nitrosylation of mouse galectin-2 prevents oxidative inactivation by hydrogen peroxide; https://cir.nii.ac.jp/crid/1360848656931317632; Identification of a Second, Non-conserved Amino Acid That Contributes to the Unique Sugar Binding Properties of the Nematode Galectin LEC-1; https://cir.nii.ac.jp/crid/1390282679603343616
• 参照: Evidence that Caenorhabditis elegans 32-kDa beta-galactoside-binding protein is homologous to vertebrate beta-galactoside-binding lectins. cDNA cloning and deduced amino acid sequence.; https://cir.nii.ac.jp/crid/1360011144446511872; Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian beta-galactosides.; https://cir.nii.ac.jp/crid/1360292619776506368; X-ray crystal structure of the human dimeric S-Lac lectin, L-14-II, in complex with lactose at 2.9-A resolution.; https://cir.nii.ac.jp/crid/1360292620725551872; Application of reinforced frontal affinity chromatography and advanced processing procedure to the study of the binding property of a Caenorhabditis elegans galectin; https://cir.nii.ac.jp/crid/1360292621067337344; Structure of S-lectin, a developmentally regulatedvertebrate beta-galactoside-binding protein.; https://cir.nii.ac.jp/crid/1360855568756191104; Multiple soluble beta-galactoside-binding lectins from human lung.; https://cir.nii.ac.jp/crid/1361137044135192832; Oligosaccharide specificity of galectins: a search by frontal affinity chromatography; https://cir.nii.ac.jp/crid/1361137045580459136; Effect of amino acid substitution by sited-directed mutagenesis on the carbohydrate recognition and stability of human 14-kDa beta-galactoside-binding lectin.; https://cir.nii.ac.jp/crid/1361418520252991744; Soluble 14-kDa beta-galactoside-specific bovine lectin. Evidence from mutagenesis and proteolysis that almost the complete polypeptide chain is necessary for integrity of the carbohydrate recognition domain.; https://cir.nii.ac.jp/crid/1361699994671847808; Galectins: A family of animal β-galactoside-binding lectins; https://cir.nii.ac.jp/crid/1361699995688320000; God must love galectins; He made so many of them; https://cir.nii.ac.jp/crid/1361699996231365120; Sugar Binding Properties of the Two Lectin Domains of the Tandem Repeat-type Galectin LEC-1 (N32) of Caenorhabditis elegans; https://cir.nii.ac.jp/crid/1361981469081367040; Introduction to galectins; https://cir.nii.ac.jp/crid/1361981469317946112; Further evidence by site-directed mutagenesis that conserved hydrophilic residues form a carbohydrate-binding site of human galectin-1; https://cir.nii.ac.jp/crid/1361981469454812416; Structure analyses of oligosaccharides by tagging of the reducing end sugars with a fluorescent compound; https://cir.nii.ac.jp/crid/1362825895009719552; Frontal Affinity Chromatography as a Tool for Elucidation of Sugar Recognition Properties of Lectins; https://cir.nii.ac.jp/crid/1363107368735641344; The Two Lectin Domains of the Tandem-Repeat 32-kDa Galectin of the Nematode Caenorhabditis elegans Have Different Binding Properties. Studies with Recombinant Protein; https://cir.nii.ac.jp/crid/1363388845584577536; Galectins as modulators of tumour progression; https://cir.nii.ac.jp/crid/1363388845945979776; X-ray Crystal Structure of the Human Galectin-3 Carbohydrate Recognition Domain at 2.1-Å Resolution; https://cir.nii.ac.jp/crid/1363670321137794304; Ah, sweet mystery of death! Galectins and control of cell fate; https://cir.nii.ac.jp/crid/1363951794795023616; Crosslinking of low-affinity glycoprotein ligands to galectin LEC-1 using a photoactivatable sulfhydryl reagent; https://cir.nii.ac.jp/crid/1364233268629536384; Purification and Characterization of β-Galactoside-Binding Proteins from Caenorhabditis elegans1; https://cir.nii.ac.jp/crid/1364233269329362176; Galectins: A Family of Animal Lectins That Decipher Glycocodes.; https://cir.nii.ac.jp/crid/1390001204932091008
• 連携機関・データベース: 国立情報学研究所 : CiNii Research; https://cir.nii.ac.jp/
• 提供元機関・データベース: Japan Link Center; https://japanlinkcenter.org/top; 雑誌記事索引データベース; https://ndlsearch.ndl.go.jp; Crossref; https://www.crossref.org; CiNii Articles; 学術機関リポジトリデータベース; https://irdb.nii.ac.jp
• 書誌ID（NDLBibID）: 8965327; http://id.ndl.go.jp/bib/8965327
• NII論文ID: 110006473475