Studies on Seed Globulins from Legumes VII. Narbonin, a 2S Globulin from Vicia narbonensis L.

Schlesier, Bernhard; Manteuffel, Renate; Rudolph, Armin; Behlke, Joachim

doi:10.1016/s0015-3796(17)30514-0

Cited by 19 publications

(17 citation statements)

References 24 publications

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“…First, Nvf32 is very similar to the V . narbonensis seed protein narbonin (Schlesier et al, 1978). It is interesting that we could not detect any VfNOD32 transcripts in preparations of broad bean seed RNA.…”

Section: Discussionmentioning

confidence: 76%

The Broad Bean Gene VfNOD32 Encodes a Nodulin with Sequence Similarities to Chitinases That Is Homologous to ([alpha]/[beta])8-Barrel-Type Seed Proteins

et al. 1996

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~Nodulin gene transcripts isolated from a broad bean (Vicia faba 1.) root nodule cDNA library and designated VfNOD32 are detectable in the nitrogen-fixing zone III of nodules and in much smaller amounts in flowers. In nodules, these transcripts are detectable for the first time 7 d after inoculation, at least 1 d before leghemoglobin gene transcription starts. Two putative full-length cDNAs representing different transcript sequences of 92.5% identity were sequenced. The corresponding broad bean genes were termed VfNOD32-A1 and VfNOD32-A2, and the encoded proteins were termed Nvf32-A1 and Nvf32-A2. The derived amino acid sequences of the Nvf32 proteins are highly homologous to the Vicia narbonensis (cu/P),-barrel seed protein narbonin. Considering this homology, Nvf32 is assumed to have a similar structure consisting of p-sheets forming a central barrel surrounded by a-helices. The two Nvf32 sequences also contain two conserved amino acid motifs that are characteristic of class-lll chitinases. Severa1 amino acids demonstrated to be essential for chitinase activity are conserved in both regions, whereas one essential glutamic acid was changed to glycine in the Nvf32-A1 isoform but not in the Nvf32-A2 isoform.

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Section: Discussionmentioning

confidence: 76%

The Broad Bean Gene VfNOD32 Encodes a Nodulin with Sequence Similarities to Chitinases That Is Homologous to ([alpha]/[beta])8-Barrel-Type Seed Proteins

et al. 1996

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“…The globulin consists of only one polypeptide chain with a relative molecular mass of 33 kDa. Its amino acid composition is very similar to that of the major storage globulins like vicilin and legumin from grain legumes (Schlesier et al 1978). Narbonin crystallizes spontaneously (Schlesier and Scholz 1974).…”

Section: Introductionmentioning

confidence: 79%

“…Narbonin, a 2S protein, was ®rst discovered as a minor component in the globulin fraction of Vicia narbonensis seeds, the narbon bean (Schlesier and Scholz 1974). The globulin consists of only one polypeptide chain with a relative molecular mass of 33 kDa.…”

Section: Introductionmentioning

confidence: 99%

Subcellular localization of the 2S globulin narbonin in seeds of Vicia narbonensis

Steffens¹,

Hải²,

Hillmer³

et al. 1997

Planta

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Narbonin is a 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons. Its amino acid composition and the pattern of its regulated accumulation in developing seeds led to the suggestion that narbonin could be a storage protein. Therefore, it was expected to be present in protein bodies of the storage tissue cells. Comparison of the cDNA-derived amino acid sequence with a directly determined partial N-terminal sequence revealed that the primary translation product of narbonin mRNA lacks a transient N-terminal signal peptide (V.H. Nong et al., 1995, Plant Mol Biol 28: 61 - 72). Narbonin polypeptides that had been synthesized in a cell-free translation system supplemented with dog pancreas microsomes were not protected against degradation by posttranslationally added proteases (protease protection assay). In accordance with the lack of a signal peptide this indicates that the polypeptide was not cotranslationally sequestered into the microsomes. The protein-body fraction that had been isolated from mature narbon bean cotyledons by a non-aqueous gradient centrifugation procedure was free of narbonin; this was found in the soluble cell fraction. In electron micrographs, narbonin could be localized in the cytoplasm using the immuno gold-labelling technique. Previously, it had already been shown that narbonin is too slowly degraded during narbon bean germination to act as a storage protein. From all these results it has to be concluded that narbonin is a cytoplasmic protein which does not belong to the storage proteins in the restricted sense. Other possible functions are discussed.

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“…Narbonin was isolated asdescribed previously [4,5]. The monoclinic crystals arc in space group P2, with cell dimensions a = 4B.9 A, b= 75.5 A, c = 50.9 A and p = l2CW.…”

Section: Methodsmentioning

confidence: 99%

“…The 2S globulin narbonin is a monomer with a single polypeptide chain and a molecular mass of about 33,000 [4,5]. Crystals ofnarbonin [6] have been used to determine its three dimensional structure at atomic resolution and to determine the primary structure during the crystallographic refinement.…”

Section: Introductionmentioning

confidence: 99%

A TIM barrel protein without enzymatic activity? Crystal‐structure of narbonin at 1.8 Å resolution

et al. 1992

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The major protein component in seeds is storage protein. These have no known enzymatic activity and a~1 to provide amino acids as a source of metabolites in the developing seedling. We report here the first three dimensional crystal structure of a seed storage globulin at high resolution. The molecule of the 15 globulin. narbonin. from Vioiu mrbonmrsis L., consisls of an eight-stranded parailei a@ barrel structure similar 15 that observed in triose phosphate isomcrasc (TIM). Narbonin is the Rrst protein with this topology possessing no known enzymatic activity, Because of the lack of sequence information most of the primary structure was determined directly from the electron density.Seed storage protein: Viciu mrhnrsis; X-ray structure; TIM barrel; Primary structure

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Studies on Seed Globulins from Legumes VII. Narbonin, a 2S Globulin from Vicia narbonensis L.

Cited by 19 publications

References 24 publications

The Broad Bean Gene VfNOD32 Encodes a Nodulin with Sequence Similarities to Chitinases That Is Homologous to ([alpha]/[beta])8-Barrel-Type Seed Proteins

The Broad Bean Gene VfNOD32 Encodes a Nodulin with Sequence Similarities to Chitinases That Is Homologous to ([alpha]/[beta])8-Barrel-Type Seed Proteins

Subcellular localization of the 2S globulin narbonin in seeds of Vicia narbonensis

A TIM barrel protein without enzymatic activity? Crystal‐structure of narbonin at 1.8 Å resolution

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