The tobacco luminal binding protein is encoded by a multigene family.

Denecke, Jürgen; Goldman, Maria Helena S.; Demolder, Jan; Seurinck, Jef; Botterman, Johan

doi:10.1105/tpc.3.9.1025

Cited by 161 publications

(23 citation statements)

References 48 publications

(44 reference statements)

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“…both with 1D3 immunoglobulins and the polyclonal antitobacco BiP serum, which matches the observation that the cloned members of the tobacco BiP family contain the Cterminal HDEL tetrapeptide (Denecke et al, 1991). Several reactive proteins with 1D3 antigenicity similar to that of the retained PAT derivatives were purified and revealed to contain significant amino acid sequence similarities with other known reticuloplasmins in mammalian cells (J.Denecke and B.Ek, in preparation).…”

supporting

confidence: 71%

“…The putative auxin receptor of maize Inohara et al, 1989;Tillman et al, 1989) and sulfhydryl endopeptidases of Vigna mungo (Akasofu et al, 1989) and Phaseolus vulgaris (Tanaka et al, 1991) contain the C-terminal KDEL peptide. In contrast, the tobacco homologue of the mammalian luminal binding protein (BiP) contains the tetrapeptide HDEL (Denecke et al, 1991). The introduction of the KDEL sequence to a vacuolar glycoprotein led to the detectable accumulation of the mutant protein in the nuclear envelope of cells from transgenic tobacco seeds (Herman et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

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Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope.

1992

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We studied protein sorting signals which are responsible for the retention of reticuloplasmins in the lumen of the plant endoplasmic reticulum (ER). A non‐specific passenger protein, previously shown to be secreted by default, was used as a carrier for such signals. Tagging with C‐terminal tetrapeptide sequences of mammalian (KDEL) and yeast (HDEL) reticuloplasmins led to effective accumulation of the protein chimeras in the lumen of the plant ER. Some single amino acid substitutions within the tetrapeptide tag (‐SDEL, ‐KDDL, ‐KDEI and ‐KDEV) can cause a complete loss of its function as a retention signal, demonstrating the high specificity of the retention machinery. However, other modifications confer efficient (‐RDEL) or partial (‐KEEL) retention. It is also shown that the efficiency of protein retention is not significantly impaired by an increased ligand concentration in plants. The efficiently retained chimeras (‐KDEL, ‐HDEL and ‐RDEL) were shown to be recognized by a monoclonal antibody directed against the C‐terminus of the mammalian reticuloplasmin protein disulfide isomerase (PDI). The recognized epitope is also present in several putative reticuloplasmins in microsomal fractions of plant and mammalian cells, suggesting that the antibodies recognize an important structural determinant of the retention signal. In addition, data are discussed which support the view that upstream sequences beyond the C‐terminal tetrapeptide can influence or may be part of the structure of reticuloplasmin retention signals.

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supporting

confidence: 71%

Section: Introductionmentioning

confidence: 99%

Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope.

1992

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“…In spite of the putative Asp glycosylation site of the 70-kD allergen in the C-terminal region, glycosylation is not likely, since the molecular mass estimated by SDS-PAGE (i.e., 70 kD) agreed well with the calculated size (i.e., 73.56 kD). Moreover, glycosylation was not detected among other BiPs identified previously [29]. …”

Section: Discussionmentioning

confidence: 87%

“…For example, polymorphism of BiP was detected in tobacco [29]and soy [30]. An isoelectric point of 4.8 was calculated from deduced amino acid sequence of Cor a 10, while the natural protein showed two isoforms at pI 5.7 and 6.1.…”

Section: Discussionmentioning

confidence: 99%

Molecular Cloning and Characterization of Hazel Pollen Protein (70 kD) as a Luminal Binding Protein (BiP): A Novel Cross-Reactive Plant Allergen

Gruehn

Suphioglu

O’Hehir

et al. 2003

Int Arch Allergy Immunol

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Background: Tree pollen contains many allergens showing cross-reactivity to proteins from pollen, seeds, and fruits of different plant species. Amongst Fagales, responsible for several allergenic responses, hazel provides the best material to study pollen as well as food allergens in one species. The aim of this study was to identify and characterize the physiological function of an allergen from hazel pollen and to determine possible cross-reactivity to proteins from hazelnut. Methods: Monoclonal antibodies (mAbs) against hazel pollen crude extract were produced. On the basis of IgE binding, demonstrated by sera from patients allergic to hazel pollen, one mAb indicating the best correlation has been selected, and the putative allergen was purified by preparative gel electrophoresis. Isoforms were investigated by two-dimensional PAGE, and for molecular identification a hazel pollen cDNA library was constructed. In situ localization of the allergen during pollen development was performed by immunofluorescence labelling. Results: Immunological staining of crude hazel pollen extract with specific IgE and mAb revealed a 70-kD protein. Immunoblot studies with mAb showed cross-reactive proteins of 70–72 kD in different plant tissues and species. After protein purification, the IgE-binding reactivity of the allergen has been reconfirmed, and two isoforms were detected. Molecular cloning identified the allergen as a luminal binding protein (BiP) of the Hsp70 family with 88–92% sequence identity in various plants. Further immunocytological studies indicated involvement of BiP during pollen development. Conclusions: Chaperons like BiP play an important role in protein synthesis and in the protection of cellular structures during stress-related processes. Because of their highly conserved protein sequences, we propose that such allergens could be responsible for at least a part of the allergenic cross-reactivity between proteins from different pollens and plant foods.

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“…Antibodies (rabbit unless otherwise indicated) were used at the following dilutions: anti-PIN1, 1:2000 [24]; anti-PIN2, 1:2000 [17]; anti-PIP2;1, 1:5000 [25]; anti-γTIP1;1, 1:5000 [26]; rat anti-SEC12, 1:1000 [27]; anti-BiP, 1:10,000 [28]; anti-ERdj3A, 1:2000 [29]; anti-ERdj3B, 1:3000 [29]; and mouse anti-Golgi mannosidase II (MannII), 1:5000 [30]. The anti-PIN1 and anti-PIN2 sera were affinity purified [31]; dilutions refer to effective dilutions of the original serum.…”

Section: Methodsmentioning

confidence: 99%

Maximum yields of microsomal-type membranes from small amounts of plant material without requiring ultracentrifugation

Abas

Luschnig

2010

Analytical Biochemistry

123

108

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Isolation of a microsomal membrane fraction is a common procedure in studies involving membrane proteins. By conventional definition, microsomal membranes are collected by centrifugation of a postmitochondrial fraction at 100,000g in an ultracentrifuge, a method originally developed for large amounts of mammalian tissue. We present a method for isolating microsomal-type membranes from small amounts of Arabidopsis thaliana plant material that does not rely on ultracentrifugation but instead uses the lower relative centrifugal force (21,000g) of a microcentrifuge. We show that the 21,000g pellet is equivalent to that obtained at 100,000g and that it contains all of the membrane fractions expected in a conventional microsomal fraction. Our method incorporates specific manipulation of sample density throughout the procedure, with minimal preclearance, minimal volumes of extraction buffer, and minimal sedimentation pathlength. These features allow maximal membrane yields, enabling membrane isolation from limited amounts of material. We further demonstrate that conventional ultracentrifuge-based protocols give submaximal yields due to losses during early stages of the procedure; that is, extensive amounts of microsomal-type membranes can sediment prematurely during the typical preclearance steps. Our protocol avoids such losses, thereby ensuring maximal yield and a representative total membrane fraction. The principles of our method can be adapted for nonplant material.

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The tobacco luminal binding protein is encoded by a multigene family.

Cited by 161 publications

References 48 publications

Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope.

Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope.

Molecular Cloning and Characterization of Hazel Pollen Protein (70 kD) as a Luminal Binding Protein (BiP): A Novel Cross-Reactive Plant Allergen

Maximum yields of microsomal-type membranes from small amounts of plant material without requiring ultracentrifugation

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