Vojnov AA, Bassi DE, Daniels MJ, Dankert MA Biosynthesis of a substituted cellulose from a mutant strain of Xanthomonas campestris Carbohydrate Research337(4) (2002)
315-326
NCBI PubMed ID:11841812 Journal NLM ID:0043535 Publisher: Elsevier Correspondence: mdankertiib.uba.ar Institutions: Instituto de Investigaciones Bioqui'micas Fundacio'n Campomar, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires and Consejo Nacional de Investigaciones Cienti'ficas y Te'cnicas, Av. Patricias Argentinas 435, 1405, Buenos Aires, Argentina
In Xanthomonas campestris the genes involved in polysaccharide (xanthan) biosynthesis are located in a gene cluster (gum) of 16 kb. A Tn5 insertion mutant with a reduced slimy phenotype has been characterized. This mutant failed to produce the pentasaccharide repeating-unit of xanthan. Only three sugars were transferred to the prenyl phosphate intermediate. Several lines of evidence suggested that the lipid-associated saccharide was the trisaccharide reducing end of the pentasaccharide from the wild-type strain. This trisaccharide was built up from UDP-Glc and GDP-Man, and a glucose residue was at the reducing end, linked to an allylic prenol through a diphosphate bridge. Results from one- or two-stage reactions showed that the trisaccharide- P--P-polyprenol was the precursor of the polymer. This new polymer, a polytrisaccharide, was detected also in vivo. The transposon responsible for the mutation was located within gumK gene. Therefore, this gene encodes for the glycosyltransferase IV, which catalyses the transfer of glucuronic acid to the lipid-linked β-D-Manp-(1→3)-β-D-Glcp-(1→4)-β-D-Glcp trisaccharide. A recombinant plasmid with the whole gum cluster restored the wild type phenotype
Methods: DNA sequencing, mild acid hydrolysis, paper chromatography, electrophoresis, radioactivity measurement, permethylation, enzymatic methods, 32P labeling Biosynthesis and genetic data: genetic data, biosynthesis data Comments, role: one of two major types of repeating units
Vojnov AA, Bassi DE, Daniels MJ, Dankert MA Biosynthesis of a substituted cellulose from a mutant strain of Xanthomonas campestris Carbohydrate Research337(4) (2002)
315-326
NCBI PubMed ID:11841812 Journal NLM ID:0043535 Publisher: Elsevier Correspondence: mdankertiib.uba.ar Institutions: Instituto de Investigaciones Bioqui'micas Fundacio'n Campomar, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires and Consejo Nacional de Investigaciones Cienti'ficas y Te'cnicas, Av. Patricias Argentinas 435, 1405, Buenos Aires, Argentina
In Xanthomonas campestris the genes involved in polysaccharide (xanthan) biosynthesis are located in a gene cluster (gum) of 16 kb. A Tn5 insertion mutant with a reduced slimy phenotype has been characterized. This mutant failed to produce the pentasaccharide repeating-unit of xanthan. Only three sugars were transferred to the prenyl phosphate intermediate. Several lines of evidence suggested that the lipid-associated saccharide was the trisaccharide reducing end of the pentasaccharide from the wild-type strain. This trisaccharide was built up from UDP-Glc and GDP-Man, and a glucose residue was at the reducing end, linked to an allylic prenol through a diphosphate bridge. Results from one- or two-stage reactions showed that the trisaccharide- P--P-polyprenol was the precursor of the polymer. This new polymer, a polytrisaccharide, was detected also in vivo. The transposon responsible for the mutation was located within gumK gene. Therefore, this gene encodes for the glycosyltransferase IV, which catalyses the transfer of glucuronic acid to the lipid-linked β-D-Manp-(1→3)-β-D-Glcp-(1→4)-β-D-Glcp trisaccharide. A recombinant plasmid with the whole gum cluster restored the wild type phenotype
Methods: DNA sequencing, mild acid hydrolysis, paper chromatography, electrophoresis, radioactivity measurement, permethylation, enzymatic methods, 32P labeling Biosynthesis and genetic data: genetic data, biosynthesis data Comments, role: one of two major types of repeating units
Related record ID(s): 8616 NCBI Taxonomy refs (TaxIDs):339 Reference(s) to other database(s): GTC:G55661NN Show glycosyltransferases
Diaz-Valencia JD, Almaraz-Barrera MJ, Arias-Romero LE, Hernandez-Rivas R, Rojo-Dominguez A, Guillen N, Vargas M The ABP-120 C-end region from Entamoeba histolytica interacts with sulfatide, a new lipid target Biochemical and Biophysical Research Communications338(3) (2005)
1527-1536
NCBI PubMed ID:16274663 Journal NLM ID:0372516 Publisher: Academic Press Institutions: Departamento de Biomedicina Molecular, Centro de Investigacion y de Estudios Avanzados del IPN, Mexico, DF, Mexico
EhABP-120 is the first filamin identified in the parasitic protozoan Entamoeba histolytica. Filamins are a family of cross-linking actin-binding proteins that promote a dynamic orthogonal web. They have been reported to interact directly with more than 30 cellular proteins and some phosphoinositides. The biochemical consequences of these interactions may have either positive or negative effects on the cross-linking function and also form a link between the cytoskeleton and plasma membrane. In this study, the EhABP-120 carboxy-terminal domain (END) was biochemically characterized. This domain was able to associate to 3-sulfate galactosyl ceramide, a new lipid target for a member of the filamin family. Also, the END domain was able to dimerize 'in vitro.' Molecular modeling analysis showed that the dimeric region is stabilized by a disulfide bond. Electrostatic and docking studies suggest that an electropositive concave pocket at the dimeric END domain interacts simultaneously with several sulfogalactose moieties of the sulfatide.
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