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The specific substance from Pneumococcus type 34 (41). The phosphodiester linkages.

ABSTRACT: 1. The phosphate groups in the type-specific substance S.34 from Pneumococcus type 34 (U.S. type 41) were shown to join the hydroxyl group at position 1 or 5 of ribitol and the hydroxyl group at position 3 of a d-galactofuranosyl residue in the next repeating unit. 2. A partial structure of the type-specific substance was derived. 3. New syntheses of d-galactose 2-phosphate and d-galactose 3-phosphate are described.

SUBMITTER: Chittenden GJ

PROVIDER: S-EPMC1186944 | biostudies-other | 1968 Oct

REPOSITORIES: biostudies-other

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The type-specific substance from Pneumococcus type 10A(34). The phosphodiester linkages.

Project description:1. The phosphate groups in the type-specific substance S. 10A from Pneumococcus type 10A (34) were shown to join the hydroxyl group at position 1 or 5 of ribitol and the hydroxyl group at position 5 or 6 of a d-galactofuranosyl residue in the next repeating unit. 2. A partial formula of the type-specific substance was derived.

| S-EPMC1265219 | biostudies-other

The specific substance from Pneumococcus type 34 the configuration of the glycosidic linkages.

Project description:1. The specific compound from Pneumococcus type 34 was isolated from capsular material by ion-exchange chromatography. This separated it from a substance with chemical and serological properties corresponding to those reported for C-substance. 2. The configuration of the two galactofuranosyl linkages in the repeating unit of S.34 was determined and the configurations previously assigned to the other glycosidic linkages were confirmed. 3. The dephosphorylated deacetylated repeating unit is thus O-beta-d-galactofuranosyl-(1-->3)-O-alpha-d-glucopyranosyl-(1-->2)-O-beta-d-galactofuranosyl-(1-->3)-O-alpha-d-galactopyranosyl- (1-->2)-ribitol.

| S-EPMC1265164 | biostudies-other

The type-specific substance from Pneumococcus type 10A(34). Structure of the dephosphorylated repeating unit.

Project description:1. A hexasaccharide unit was isolated from the specific substance S. 10A from Pneumococcus type 10A (34) by hydrolysis with alkali followed by enzymic dephosphorylation. 2. The hexasaccharide was shown to be O-d-galactofuranosyl-(1-->3)-O-d- galactopyranosyl-(1-->4)-O-[d-galactofuranosyl- (1-->6)]-O-2-acet-amido-2-deoxy-d-galactopyranosyl- (1-->3)-O-d-galactopyranosyl-(1-->2)-ribitol.

| S-EPMC1265218 | biostudies-other

The type-specific substance from Pneumococcus type 33B.

Project description:1. The type-specific substance, S. 33B, from Pneumococcus type 33B contains P, 2.89; hexose, 51; total sugar, 69; galactosamine, 18; and d-glucose, 20%. 2. After degradation with alkali, followed by enzymic dephosphorylation, S. 33B yielded a hexasaccharide. 3. The hexasaccharide was assigned the structure O-beta-d-glucopyranosyl- (1-->5)-O-beta-d-galactofuranosyl- (1-->3)-O-2-acetamido-2-deoxy-beta-d- galactopyranosyl-(1-->4)-O-[alpha-d- galactopyranosyl-(1-->2)]-alpha-d-galactopyranosyl- (1-->2)-ribitol. 4. Phosphate residues in S. 33B are located on the hydroxyl groups at position 5 of ribitol units and on the hydroxyl groups at position 6 of hexopyranose residues.

| S-EPMC1166164 | biostudies-other

The type-specific substance from Pneumococcus type 29.

Project description:1. A pentasaccharide, corresponding to the dephosphorylated repeating unit of the specific substance, S.29, from Pneumococcus type 29, was obtained by hydrolysis with alkali followed by enzymic dephosphorylation. 2. The pentasaccharide was shown to be O-2-acetamido-2-deoxy-beta-d-galactopyranosyl-(1-->6)-O-beta-d-galactofuranosyl-(1-->3)-O-beta-d-galactopyranosyl-(1-->6)-O-beta-d-galactofuranosyl-(1-->1)-ribitol. 3. The phosphodiester linkages in S.29 join the hydroxyl group at position 5 of ribitol and the hydroxyl group at position 3 or 4 of a 2-acetamido-2-deoxy-d-galactose residue in the next repeating unit. 4. A partial structure for S.29 was deduced from these experiments.

| S-EPMC1187575 | biostudies-other

The type-specific substance from Pneumococcus type 13.

Project description:1. The type-specific substance, S.13, from Pneumococcus type 13 was subjected to hydrolysis with alkali, followed by enzymic dephosphorylation, to yield a pentasaccharide. 2. The pentasaccharide, corresponding to the dephosphorylated repeating unit of S.13, was shown to be O-beta-d-galactopyranosyl-(1-->4)-O-beta- d-glucopyranosyl-(1-->3)-O-beta-d- galactofuranosyl-(1-->4)-O-2-acetamido-2-deoxy-beta-d- glucopyranosyl-(1-->2)-ribitol. 3. The phosphodiester linkages in S.13 join the hydroxyl group at position 1 of ribitol and the hydroxyl group at position 4 of a galactopyranosyl residue in the next repeating unit. 4. Ester groups, presumably O-acetyl, are located on positions 2 or 3 of most glucopyranosyl residues in S.13. 5. A partial structure for S.13 is proposed.

| S-EPMC1174299 | biostudies-other

The type-specific substance from Pneumococcus type 11A(43).

Project description:1. The type-specific substance from Pneumococcus type 11A(43) is a polymer containing d-glucose, d-galactose, glycerol, phosphate and O-acetyl in the approximate molecular proportions 2:2:1:1:2. 2. Removal of the O-acetyl groups with ammonia gave a compound no longer active towards type 11A antiserum. 3. Treatment of S.11A with sodium borohydride, followed by hydrolysis with alkali yielded a phosphorus-free polysaccharide, whose structure was studied by methylation and by degradation with periodate. 4. Examination of S.11A and its de-O-acetyl derivative by periodate oxidation led to the partial structure (XI) for the type-specific substance, which thus has several features in common with S.18.

| S-EPMC1185066 | biostudies-other

Strand-specific (asymmetric) contribution of phosphodiester linkages on RNA polymerase II transcriptional efficiency and fidelity.

Project description:Nonenzymatic RNA polymerization in early life is likely to introduce backbone heterogeneity with a mixture of 2'-5' and 3'-5' linkages. On the other hand, modern nucleic acids are dominantly composed of 3'-5' linkages. RNA polymerase II (pol II) is a key modern enzyme responsible for synthesizing 3'-5'-linked RNA with high fidelity. It is not clear how modern enzymes, such as pol II, selectively recognize 3'-5' linkages over 2'-5' linkages of nucleic acids. In this work, we systematically investigated how phosphodiester linkages of nucleic acids govern pol II transcriptional efficiency and fidelity. Through dissecting the impacts of 2'-5' linkage mutants in the pol II catalytic site, we revealed that the presence of 2'-5' linkage in RNA primer only modestly reduces pol II transcriptional efficiency without affecting pol II transcriptional fidelity. In sharp contrast, the presence of 2'-5' linkage in DNA template leads to dramatic decreases in both transcriptional efficiency and fidelity. These distinct effects reveal that pol II has an asymmetric (strand-specific) recognition of phosphodiester linkage. Our results provided important insights into pol II transcriptional fidelity, suggesting essential contributions of phosphodiester linkage to pol II transcription. Finally, our results also provided important understanding on the molecular basis of nucleic acid recognition and genetic information transfer during molecular evolution. We suggest that the asymmetric recognition of phosphodiester linkage by modern nucleic acid enzymes likely stems from the distinct evolutionary pressures of template and primer strand in genetic information transfer during molecular evolution.

| S-EPMC4136571 | biostudies-literature

Artificial bioconjugates with naturally occurring linkages: the use of phosphodiester.

Project description:Artificial orthogonal bond formations such as the alkyne-azide cycloaddition have enabled selective bioconjugations under mild conditions, yet naturally occurring linkages between native functional groups would be more straightforward to elaborate bioconjugates. Herein, we describe the use of a phosphodiester bond as a versatile option to access various bioconjugates. An opposite activation strategy, involving 5'-phosphitylation of the supported oligonucleotides, has allowed several biomolecules that possess an unactivated alcohol to be directly conjugated. It should be noted that there is no need to pre-install artificial functional groups and undesired and unpredictable perturbations possibly caused by bioconjugation can be minimized.

| S-EPMC6071721 | biostudies-literature

Template-directed chemical ligation to obtain 3'-3' and 5'-5' phosphodiester DNA linkages.

Project description:Up to now, the direct ligation of two DNA fragments with opposite directions to obtain 3'-3' or 5'-5' phosphate ester bonds is still challenging. The only way to obtain DNA oligonucleotides containing a 3'-3' or 5'-5' inversion of polarity sites is based on professional DNA chemical synthesis. Herein, we demonstrate a convenient template-directed chemical ligation that enables 3'-3' and 5'-5' linkages of two DNA oligonucleotides. This method is based on the assembly of two oligonucleotides on a template in opposite directions through forming antiparallel and parallel duplexes simultaneously, followed by coupling with N-Cyanoimidazole under mild condition. Moreover, on the basis of DNA oligonucleotides with 5'-5' linkage obtained through our template-directed chemical ligation, we developed a new cDNA display technique for in vitro selection of functional polypeptides.

| S-EPMC3975322 | biostudies-literature

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