Disease relevance of Sorghum

• Cloning of three A-type cytochromes P450, CYP71E1, CYP98, and CYP99 from Sorghum bicolor (L.) Moench by a PCR approach and identification by expression in Escherichia coli of CYP71E1 as a multifunctional cytochrome P450 in the biosynthesis of the cyanogenic glucoside dhurrin [1].
• Results indicated that the amino terminus was blocked by an acetyl group, as has previously been found for the coat protein of Johnsongrass mosaic potyvirus [2].
• The acute toxicities of lead (Pb) and copper (Cu) to important crop plants Sorghum bicolor, Cucumis sativus, Triticum aestivum, and Zea mays were compared [3].
• The basal diet contained (dry matter basis) 10.1% sudangrass hay, 34.9% alfalfa hay, 43.9% steam flaked corn, 6.1% molasses, 4.0% fat, .46% urea, .49% trace mineral salt, 33 mg/kg lasalocid and 2,200 IU/kg vitamin A. Dry matter intake was limited to 1.65% of body weight [4].

High impact information on Sorghum

• Finally, comparative analysis of the gene composition in barley, wheat (Triticum aestivum), rice (Oryza sativa), and sorghum (Sorghum bicolor) suggested massive gene movements at the Rph7 locus in the Triticeae lineage [5].
• Isolation of the heme-thiolate enzyme cytochrome P-450TYR, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench [6].
• The cytochrome P-450 enzyme (hemethiolate enzyme) that catalyzes the N-hydroxylation of L-tyrosine to N-hydroxytyrosine, the committed step in the biosynthesis of the cyanogenic glucoside dhurrin, has been isolated from microsomes prepared from etiolated seedlings of Sorghum bicolor (L.) Moench [6].
• Based upon the results of a Cot analysis, hydroxyapatite chromatography was used to fractionate sorghum (Sorghum bicolor) genomic DNA into highly repetitive (HR), moderately repetitive (MR), and single/low-copy (SL) sequence components that were consequently cloned to produce HRCot, MRCot, and SLCot genomic libraries [7].
• NMR analyses of the labeling pattern obtained using various 13C-labeled precursors indicated that both the lipid tail and the quinone head of sorgoleone, the main allelopathic component of the oily root exudate of Sorghum bicolor, were derived from acetate units, but that the two moieties were synthesized in different subcellular compartments [8].

Biological context of Sorghum

• The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor. Isolation, cloning, heterologous expression, and substrate specificity [9].
• The specificity of the interaction was investigated using a competitive binding assay to compare directly the affinities of various proteins and synthetic polymers for the tannin obtained from Sorghum bicolor (Lin.) Moench [10].
• The gene specifying plastid transketolase (TK) of maize (Zea mays) was cloned from a cDNA library by southern blotting using a heterologous probe from sorghum (Sorghum bicolor) [11].
• To investigate the extent of this differential gene expression and thus gain insight into the genetic basis of C4 photosynthesis, genes that are differentially expressed in the mesophyll and bundle-sheath cells were catalogued in the NADP-malic enzyme type C4 grass Sorghum bicolor [12].
• Highly purified fractions of chorismate mutase 1 and 2 from etiolated seedlings of Sorghum bicolor were used as the antigen for antibody production in BALB/c mice [13].

Anatomical context of Sorghum

• A crude polysaccharide that hemolyzed human red blood cells of the ABO types was isolated from the condensed tannin fraction of Sorghum bicolor [14].
• The Sorghum bicolor atp6-1 gene and chimeric atp6 genes with additional maize sequences were introduced into isolated maize mitochondria via electroporation [15].

Associations of Sorghum with chemical compounds

• A microsomal fraction from seedlings of Sorghum bicolor (Linn) Moench has been shown to catalyze the conversion of L-tyrosine to p-hydroxymandelonitrile via p-hydroxyphenylacetaldoxime [16].
• The biosynthesis of cyanogenic glucosides in higher plants. The (E)- and (Z)-isomers of p-hydroxyphenylacetaldehyde oxime as intermediates in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench [17].
• The biosynthesis of cyanogenic glucosides in higher plants. N-Hydroxytyrosine as an intermediate in the biosynthesis of dhurrin by Sorghum bicolor (Linn) Moench [18].
• Isolation and reconstitution of the heme-thiolate protein obtusifoliol 14alpha-demethylase from Sorghum bicolor (L.) Moench [19].
• In marked contrast to an analogous pathway in Sorghum bicolor, p-hydroxyphenylacetonitrile is the best substrate for cyanide production (Vmax = 224 nmol/h/g, fresh wt) and the physiological substrate tyrosine is the poorest (Vmax = 18.8 nmol/h/g, fresh wt) [20].

Gene context of Sorghum

• Characterization of a Sorghum bicolor gene family encoding putative protein kinases with a high similarity to the yeast SNF1 protein kinase [21].
• In contrast, when a Sorghum bicolor atp6 gene was introduced into isolated maize mitochondria, the gene was transcribed, but the RNA was not edited, although all the editing sites in maize and sorghum atp6 RNA are identical [22].
• Cloning and expression analysis of CRY2 gene in Sorghum bicolor [23].
• Cytochrome P-450TYR, which catalyzes the N-hydroxylation of L-tyrosine in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench has recently been isolated (Sibbesen, O., Koch, B., Halkier, B. A., and Møller, B. L. (1994) Proc. Natl. Acad. Sci. U.S.A. 92, 9740-9744) [24].
• Novel cyanogenic plants have been generated by the simultaneous expression of the two multifunctional sorghum (Sorghum bicolor [L.] Moench) cytochrome P450 enzymes CYP79A1 and CYP71E1 in tobacco (Nicotiana tabacum cv Xanthi) and Arabidopsis under the regulation of the constitutive 35S promoter [25].

Analytical, diagnostic and therapeutic context of Sorghum

• Molecular cloning of hydroxynitrile lyase from Sorghum bicolor (L.). Homologies to serine carboxypeptidases [26].

References