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PubMed1989

Comparison of glycerolipid biosynthesis in non-green plastids from sycamore (Acer pseudoplatanus) cells and cauliflower (Brassica oleracea) buds.

The availability of methods to fractionate non-green plastids and to prepare their limiting envelope membranes [Alban, Joyard & Douce (1988) Plant Physiol. 88, 709-717] allowed a detailed analysis of the biosynthesis of lysophosphatidic acid, phosphatidic acid, diacylglycerol and monogalactosyl-diacylglycerol (MGDG) in two different types of non-green starch-containing plastids: plastids isolated from cauliflower buds and amyloplasts isolated from sycamore cells. An enzyme [acyl-ACP (acyl carrier protein):sn-glycerol 3-phosphate acyltransferase) recovered in the soluble fraction of non-green plastids transfers oleic acid from oleoyl-ACP to the sn-1 position of sn-glycerol 3-phosphate to form lysophosphatidic acid. Then a membrane-bound enzyme (acyl-ACP:monoacyl-sn-glycerol 3-phosphate acyltransferase), localized in the envelope membrane, catalyses the acylation of the available sn-2 position of 1-oleoyl-sn-glycerol 3-phosphate by palmitic acid from palmitoyl-ACP. Therefore both the soluble phase and the envelope membranes are necessary for acylation of sn-glycerol 3-phosphate. The major difference between cauliflower (Brassica oleracea) and sycamore (Acer pseudoplatanus) membranes is the very low level of phosphatidate phosphatase activity in sycamore envelope membrane. Therefore, very little diacylglycerol is available for MGDG synthesis in sycamore, compared with cauliflower. These findings are consistent with the similarities and differences described in lipid metabolism of mature chloroplasts from 'C18:3' and 'C16:3' plants (those with MGDG containing C18:3 and C16:3 fatty acids). Sycamore contains only C18 fatty acids in MGDG, and the envelope membranes from sycamore amyloplasts have a low phosphatidate phosphatase activity and therefore the enzymes of the Kornberg-Pricer pathway have a low efficiency of incorporation of sn-glycerol 3-phosphate into MGDG. By contrast, cauliflower contains MGDG with C16:3 fatty acid, and the incorporation of sn-glycerol 3-phosphate into MGDG by the enzymes associated with envelope membranes is not limited by the phosphatidate phosphatase. These results demonstrate that: (1) non-green plastids employ the same biosynthetic pathway as that previously established for chloroplasts (the formation of glycerolipids is a general property of all plastids, chloroplasts as well as non-green plastids), (2) the envelope membranes are the major structure responsible for the biosynthesis of phosphatidic acid, diacylglycerol and MGDG, and (3) the enzymes of the envelope Kornberg-Pricer pathway have the same properties in non-green starch-containing plastids as in mature chloroplasts from C16:3 and C18:3 plants.

Acyltransferases↗
PubMed2000

Variation and selection at the CAULIFLOWER floral homeotic gene accompanying the evolution of domesticated Brassica oleracea.

The evolution of plant morphologies during domestication events provides clues to the origin of crop species and the evolutionary genetics of structural diversification. The CAULIFLOWER gene, a floral regulatory locus, has been implicated in the cauliflower phenotype in both Arabidopsis thaliana and Brassica oleracea. Molecular population genetic analysis indicates that alleles carrying a nonsense mutation in exon 5 of the B. oleracea CAULIFLOWER (BoCAL) gene are segregating in both wild and domesticated B. oleracea subspecies. Alleles carrying this nonsense mutation are nearly fixed in B. oleracea ssp. botrytis (domestic cauliflower) and B. oleracea ssp. italica (broccoli), both of which show evolutionary modifications of inflorescence structures. Tests for selection indicate that the pattern of variation at this locus is consistent with positive selection at BoCAL in these two subspecies. This nonsense polymorphism, however, is also present in both B. oleracea ssp. acephala (kale) and B. oleracea ssp. oleracea (wild cabbage). These results indicate that specific alleles of BoCAL were selected by early farmers during the domestication of modified inflorescence structures in B. oleracea.

Base Sequence↗
PubMed2003

Dual subcellular distribution of cytochrome b5 in plant, cauliflower, cells.

Subfractionation studies showed that cytochrome b(5) (cyt b5), which has been considered to be a typical ER protein, was localized in both the endoplasmic reticulum membrane (ER) and the outer membrane of mitochondria in cauliflower (Brassica olracea) cells and was a component of antimycin A-insensitive NADH-cytochrome c reductase system in both membranes. When cDNA for cauliflower cyt b5 was introduced into mammalian (COS-7) and yeast cells as well as into onion cells, the expressed cytochrome was localized both in the ER and mitochondria in those cells. On the other hand, rat and yeast cyt b5s were specifically localized in the ER membranes even in the onion cells. Mutation experiments showed that cauliflower cyt b5 carries information that targets it to the ER and mitochondria within the carboxy-terminal 10 amino acids, as in the case of rat and yeast cyt b5s, and that replacement of basic amino acids in this region of cauliflower cyt b5 with neutral or acidic ones resulted in its distribution only in the ER. Together with the established findings of the importance of basic amino acids in mitochondrial targeting signals, these results suggest that charged amino acids in the carboxy-terminal portion of cyt b5 determine its location in the cell, and that the same mechanism of signal recognition and of protein transport to organelles works in mammalian, plant, and yeast cells.

Amino Acids, Basic↗
PubMedDate not supplied

Duplication of the Brassica oleracea APETALA1 floral homeotic gene and the evolution of domesticated cauliflower.

Development of the cauliflower phenotype in Arabidopsis thaliana requires mutations at both the CAULIFLOWER and APETALA1 loci. BoAP1 is the Brassica oleracea orthologue to the Arabidopsis AP1 gene, and is present in two copies in Brassica genomes. The BoAP1-A gene appears to encode a full-length protein, but BoAP1-B alleles in B. oleracea contain insertions that lead to premature translation termination. The BoAP1-B allele found in most B. oleracea subspecies, including B. oleracea ssp. botrytis (domesticated cauliflower) contains a 9 bp insertion in exon 4. This insertion leads to the formation of an in-frame translation termination codon, and these alleles can encode a protein that is truncated at the K domain of this MADS-box transcriptional activator. The allele in B. oleracea ssp. oleracea (wild cabbage) lacks this insertion and instead contains a downstream 4 bp frameshift mutation resulting in the formation of a nonsense mutation. The structure of the BoAP1-B alleles suggests that they are impaired in their ability to perform their floral meristem identity function. These mutations, in conjunction with mutations at the BoCAULIFLOWER (BoCAL) locus, may be associated with the evolution of domesticated cauliflower.

Alleles↗
PubMed1997

Inositol 1,4,5-trisphosphate-sensitive Ca2+ release across nonvacuolar membranes in cauliflower.

Previous studies have indicated that the vacuole represents the major inositol 1,4,5-trisphosphate (InsP3)-mobilizable Ca2+ pool in higher plants. This findings is in contrast to animal cells, in which the endoplasmic reticulum and plasma membrane constitute the dominant InsP3-sensitive membranes. We used membrane vesicles prepared from cauliflower (Brassica oleracae L.) inflorescences that were separated on continuous sucrose gradients to demonstrate that cauliflower possesses at least two distinct membrane populations that are sensitive to InsP3. One of these membrane populations in nonvacuolar in origin and relies upon a Ca(2+)-ATPase to accumulate Ca2+. In addition, we have shown that two polyclonal antibodies, raised against peptides corresponding to the animal type 1 InsP3 receptor, recognize immunologically related proteins in cauliflower, and that the distribution of immunoreactive proteins on a linear sucrose gradient reinforces the notion that cauliflower contains more than one membrane subtype that is sensitive to InsP3. To our knowledge, this is the first report describing an InsP3-sensitive Ca2+ store other than the vacuole in higher plant cells.

Amino Acid Sequence↗
PubMed1991

Opium addiction and cauliflower ears: a case report.

The case of an elderly Chinese male opium addict with cauliflower ears is discussed. He had no history of contact sports that could have led to auricular trauma resulting in deformed ears. Besides cauliflower ears, he had features of chronic bronchitis. The association between opium addiction and cauliflower ears was first described way back in 1932. It was attributed to the prolonged opium induced sleep on hard surface subjecting the ears to repeated pressure and trauma. With the changing pattern of drug abuse, opium abuse related cauliflower ears will become a vanishing sign.

Aged↗
PubMed1982

Persistence of carbaryl residues in and on unprocessed and processed cauliflower curds.

Carbaryl was applied three times at 15 days interval to cauliflower (Brassica oleracea var. botrytis L.), and its persistence was determined spectrophotometrically at 0, 1, 3, 6, 10, and 15 days after the first and last treatments. In unprocessed cauliflower the prescribed tolerance level for carbaryl residues of 5 ppm was only reached on the sixth day, in processed cauliflower on the third day after application. Pretreatment with washing + boiling/cooking on the other hand led to a considerable decrease of the carbaryl residues already on the day of application. The lower carbaryl values encountered in all variants after the last application are attributed by the authors to a thinning effect due to an increased cauliflower mass.

Brassica↗
PubMed1982

Identification by immunoprecipitation of cauliflower mosaic virus in vitro major translation product with a specific serum against viroplasm protein.

A highly specific antiserum was prepared against purified cauliflower mosaic virus viroplasm-protein (VmP). A virus specific in vitro major translation product (TPmaj), encoded by the 19S poly(A) RNA fraction from cauliflower mosaic virus infected turnip leaves, was recognized by this antiserum. The N-terminal sequence of TPmaj corresponds to the sequence following the first in-phase initiation codon in gene VI of the cauliflower mosaic virus genome. Both VmP and TPmaj have blocked termini and probably start from the same AUG codon.

Journal Article↗
PubMed2002

Third position codon composition suggests two classes of genes within the Cauliflower mosaic virus genome.

The translation of viral mRNAs by host ribosomes is essential for infection. Hence, codon usage of virus genes may influence efficiency of infection. In addition, composition of nucleotides in the third position within codons of genes can reflect evolutionary relationships. In this study, third position codon composition was examined for the seven genes of eight Cauliflower mosaic virus isolates. Genes IV-VII had similar codon composition values and were termed Class 1 genes. Genes I-III possessed corresponding codon composition values and were termed Class 2 genes. The codon composition values of Class 1 and genes differed significantly. Neither Class 1 nor Class 2 genes had codon composition values identical to that of the host plant, Arabidopsis thaliana. However, Class 1 genes possessed codon composition values closer to those of the host than Class 2 genes. Examination of the genomes of three Rous sarcoma virus isolates indicated that codon composition values were similar for the gag, pol, and env genes but these genes differed significantly from the src genes. Since codon composition values for Rous sarcoma virus distinguished a "foreign" gene from the rest of the viral genome, it is possible that the Cauliflower mosaic virus genome is composed of genes from two different sources. Others have suggested that Cauliflower mosaic virus evolved in this manner and our data provide support for this hypothesis.

Arabidopsis↗
PubMed1992

Analysis of cauliflower mosaic virus RNAs in Brassica species showing a range of susceptibility to infection.

Cauliflower mosaic virus (CaMV) is a plant pararetrovirus i.e., a DNA virus that replicates through reverse transcription of its terminally redundant genomic RNA (the 35 S RNA). In this study, the absolute levels and relative ratios of CaMV-encoded RNA species were analyzed in Brassica host plants with different susceptibilities to infection. As reported previously, only very low levels of CaMV RNAs were detected in plants of low susceptibility such as cauliflower. Early in infection, a large proportion of these RNAs were the "short-stop" RNA: a 180-nucleotide RNA generated by mRNA 3' end processing at the first encounter of the polyadenylation [poly(A)] signal rather than at the second encounter by which the 35 S RNA is generated. In contrast, in highly susceptible plants such as turnip, high levels of CaMV RNAs were detected, and the short-stop RNA represented only a small fraction of the RNA. In leaf protoplasts, bypass of the poly(A) signal was similar in all Brassica species. Finally, the ratio of the 19 S RNA, a subgenomic RNA encoding a post-transcriptional trans-activator, to the 35 S RNA was lower in cauliflower than in turnip. These results are discussed in light of the CaMV life cycle.

Brassica↗
PubMed1994

Glucose- and ADPGlc-dependent starch synthesis in isolated cauliflower-bud amyloplasts. Analysis of the interaction of various potential precursors.

Recently, we have demonstrated that isolated cauliflower-bud amyloplasts incorporate glucose 6-phosphate at high rates into newly synthesized starch (Neuhaus et al. (1993) Plant Physiol. 101, 573-578). Here we have analyzed the incorporation of radioactively labeled glucose and ADPglucose into newly synthesized starch. It could be shown that glucose incorporation into starch exhibits a typical substrate saturation behaviour and is linear with time for at least 40 min. The incorporation of glucose is strongly dependent upon the intactness of the plastids and upon the presence of both, ATP and 3-phosphoglyceric acid. Using 4,4'-diisothiocyanostilbene-2,2'-disulfonate (DIDS) we showed that glucose is taken up into isolated cauliflower-bud amyloplasts as the free glucose molecule, rather than as glucose 6-phosphate. Glucose incorporation into newly synthesized starch is strongly inhibited in the presence of low concentrations of glucose 6-phosphate. The radioactively labeled glucose moiety of ADPglucose is also incorporated into starch. This incorporation can be saturated at increased concentrations of ADPglucose. ATP significantly inhibits the incorporation of the glucose moiety of ADPglucose into starch. This inhibition can be reinforced by the additional presence of glucose 6-phosphate. Glucose 6-phosphate-dependent starch synthesis is not strongly inhibited in the presence of glucose or ADPglucose indicating that glucose 6-phosphate is the precursor for starch synthesis in isolated cauliflower-bud amyloplasts.

Adenosine Diphosphate Glucose↗
PubMed2003

Valorization of cauliflower (Brassica oleracea L. var. botrytis) by-products as a source of antioxidant phenolics.

The present study reports the development of two extraction protocols, with potential industrial applicability, to valorize cauliflower (Brassica oleracea L. var. botrytis) byproducts as a source of antioxidant phenolics. In addition, the nonionic polystyrene resin Amberlite XAD-2 was used to obtain purified extracts. The extract yield, phenolic content, phenolic yield, and correlation between the antioxidant activity and the phenolic content were studied. The water and ethanol protocols yield a phenolic content of 33.8 mg/g freeze-dried extract and 62.1 mg/g freeze-dried extract, respectively. This percentage increased considerably when the extracts were purified using Amberlite XAD-2 yielding a phenolic content of 186 mg/g freeze-dried extract (water extract) and 311.1 mg/g freeze-dried extract (ethanol extract). Cauliflower byproduct extracts showed significant free radical scavenging activity (vs both DPPH(*) and ABTS(*)(+) radicals), ferric reducing ability (FRAP assay), and capacity to inhibit lipid peroxidation (ferric thiocyanate assay). In addition, the antioxidant activity was linearly correlated with the phenolics content. The results obtained indicate that the cauliflower byproducts are a cheap source of antioxidant phenolics very interesting from both the industrial point of view and the possible usefulness as ingredients to functionalize foodstuffs.

Antioxidants↗
PubMed2003

N-linked glycosylation of native and recombinant cauliflower xyloglucan endotransglycosylase 16A.

The gene encoding a XET (xyloglucan endotransglycosylase) from cauliflower ( Brassica oleracea var. botrytis ) florets has been cloned and sequenced. Sequence analysis indicated a high degree of similarity to other XET enzymes belonging to glycosyl hydrolase family 16 (GH16). In addition to the conserved GH16 catalytic sequence motif EIDFE, there exists one potential N-linked glycosylation site, which is also highly conserved in XET enzymes from this family. Purification of the corresponding protein from extracts of cauliflower florets allowed the fractionation of a single, pure glycoform, which was analysed by MS techniques. Accurate protein mass determination following the enzymic deglycosylation of this glycoform indicated the presence of a high-mannose-type glycan of the general structure GlcNAc2Man6. LC/MS and MS/MS (tandem MS) analysis provided supporting evidence for this structure and confirmed that the glycosylation site (underlined) was situated close to the predicted catalytic residues in the conserved sequence YLSSTNNEHDEIDFEFLGNRTGQPVILQTNVFTGGK. Heterologous expression in Pichia pastoris produced a range of protein glycoforms, which were, on average, more highly mannosylated than the purified native enzyme. This difference in glycosylation did not influence the apparent enzymic activity of the enzyme significantly. However, the removal of high-mannose glycosylation in recombinant cauliflower XET by endoglycosidase H, quantified by electrospray-ionization MS, caused a 40% decrease in the transglycosylation activity of the enzyme. No hydrolytic activity was detected in native or heterologously expressed BobXET16A, even when almost completely deglycosylated.

Amino Acid Sequence↗
PubMed1995

Analysis of carbohydrate transport across the envelope of isolated cauliflower-bud amyloplasts.

Using isolated amyloplasts from cauliflower buds, we have characterized the interaction and transport of various carbohydrates across the envelope membrane of a heterotrophic plastid. According to our results, glucose 6-phosphate (Glc6P) and glucose 1-phosphate (Glc1P) do not share the same transport protein for uptake into cauliflower-bud amyloplasts. Glc6P-dependent starch synthesis is strongly inhibited in the presence of dihydroxyacetone phosphate (DHAP) or 4,4'-di-isothiocyano-2,2'- stilbenedisulphonic acid (DIDS), whereas Glc1P-dependent starch synthesis is hardly affected by these compounds. Analysis of the Glc6P uptake into proteoliposomes reconstituted from the envelope proteins of cauliflower-bud amyloplasts indicate that Glc6P is taken up in a counter-exchange mode with Pi, DHAP or Glc6P, whereas Glc1P does not act as a counter-exchange substrate. Pi is a strong competitive inhibitor of Glc6P uptake (Ki 0.8 mM) into proteoliposomes, whereas Glc1P does not significantly inhibit Glc6P transport. Beside a hexose-phosphate translocator, these amyloplasts possess an envelope protein mediating the transport of glucose across the membrane. This translocator exhibits an apparent Km for glucose of 2.2 mM and is inhibited by low concentrations of phloretin, known to be a specific inhibitor of glucose-transport proteins. Maltose inhibits the uptake of glucose (Ki 2.3 mM), indicating that both carbohydrates share the same translocator.

Biological Transport↗
PubMed1997

A structure-specific endonuclease from cauliflower (Brassica oleracea var. botrytis) inflorescence.

A protein with structure-specific endonuclease activity has been purified to near homogeneity from cauliflower ( Brassica oleracea var. botrytis) inflorescence through five successive column chromatographies. The protein is a single polypeptide with a molecular mass of 40 kDa. Using three different branched DNA structures (flap, pseudo-Y and stem-loop) we found that the enzyme, a cauliflower structure-specific endonuclease, cleaved the single-stranded tail in the 5'-flap and 5'-pseudo-Y structures, whereas it could not incise the 3'-flap and 3'-pseudo-Y structures. The incision points occur around the single strand-duplex junction in these DNA substrates and the enzyme leaves 5'-PO4 and 3'-OH termini on DNA. The protein also endonucleolytically cleaves on the 3'-side of the single-stranded region at the junction of unpaired and duplex DNA in the stem-loop structure. The structure-specific endonuclease activity is stimulated by Mg2+ and by Mn2+, but not by Ca2+. Like mammalian FEN-1, the protein has weak 5'-->3' double-stranded DNA-specific exonuclease activity. These results indicate that the cauliflower protein is a plant structure-specific endonuclease like mammalian FEN-1 or may be the plant alternative.

Brassica↗
PubMed1991

Chloroplast DNA topoisomerase I from cauliflower.

An ATP-independent DNA topoisomerase has been isolated from chloroplasts of cauliflower leaves (Brassica oleracea var. botrytis) through DEAE-cellulose, AF-blue Toyopearl, and hydroxyapatite column chromatography. The sedimentation coefficient and Stokes radius of this enzyme are 3.6S and 3.6 nm, respectively, and the molecular weight of native enzyme is estimated to be 54,000. This enzyme changes the linking number in steps of one. The enzyme activity is stimulated by MgCl2, and this enzyme shows optimum activity at 30 degrees C in the range of 3 mM MgCl2 + 100 mM KCl-10 mM MgCl2 + 50 mM KCl. The enzyme activity was reduced remarkably by N-ethylmaleimide, indicating that a free sulfhydryl group is important for the activity; heparin and ellipticine also reduced the activity. Both cauliflower chloroplast topoisomerase and spinach chloroplast topoisomerase can relax positive supercoils as well as negative supercoils. From these properties, cauliflower chloroplast topoisomerase can be classified as a eukaryotic type I DNA topoisomerase.

Chloroplasts↗
PubMed1993

Modification of Phospholipid Catabolism in Microsomal Membranes of [gamma]-Irradiated Cauliflower (Brassica oleracea L.).

Acceleration of membrane deterioration has been observed recently during storage of [gamma]-irradiated cauliflower (Brassica oleracea L., Botrytis group). In the present study, the activity of microsome-associated lipolytic enzymes was investigated in cauliflower florets exposed to 0 or 4 kilograys of [gamma] radiation and stored for 8 d at 13[deg]C. Radiolabeled breakdown products obtained from the metabolism of (16:0/18:2*)-phosphatidylcholine and (16:0/16:0)-phosphatidyl-[N-methyl-3H]choline by microsomal membranes indicated that phospholipase D (EC 3.1.4.4), phosphatidic acid phosphatase (EC 3.1.3.4), and lipolytic acyl hydrolase were associated with the membranes. The rate of phosphatidylcholine catabolism by the membranes increased slowly in control cauliflower during storage. [gamma] irradiation caused an immediate rise in phosphatidylcholine catabolism that remained higher than that of the controls during subsequent storage. Collectively, the data suggest that enhancement of membrane lipolytic activity results from free-radical-induced stress. Rapid increase of the membrane-associated phospholipase D activity may be a key event leading to accelerated membrane deterioration following [gamma] irradiation.

Journal Article↗
PubMed1976

Purification and Characterization of DNA-dependent RNA Polymerases from Cauliflower Nuclei.

DNA-dependent RNA polymerases were solubilized from nuclei of cauliflower inflorescences and purified by agarose A-1.5m, DEAE-cellulose, DEAE-Sephadex, and phosphocellulose chromatography and sucrose density gradient centrifugation. RNA polymerases I + III were separated from II by DEAE-cellulose chromatography. Subsequent chromatography on DEAE-Sephadex resolved RNA polymerase I from III. RNA polymerases I and II were further purified to high specific activity by phosphocellulose chromatography and sucrose density gradient centrifugation. RNA polymerase I was refractory to alpha-amanitin at 2 mg/ml. RNA polymerase II was 50% inhibited at 0.05 mug/ml, and RNA polymerase III was 50% inhibited at 1 to 2 mg/ml of alpha-amanitin. The enzymes were characterized with respect to divalent cation optima, ionic strength optima, and abilities to transcribe cauliflower, synthetic, and cauliflower mosaic virus DNA templates.

Journal Article↗