Lectin-like activity of lupin seed conglutin γ, a glycoprotein previously referred to as a storage protein

Duranti, Marcello; Gius, Cristina; Scarafoni, Alessio

doi:10.1093/jxb/46.6.725

Cited by 18 publications

(26 citation statements)

References 19 publications

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“…A similar process occurs for a minor basic 7 s globulin of soybean (Bg7S ; Hirano et al, 1992). A lectin-like activity of conglutin y has been detected very recently (Duranti et al, 1995).…”

mentioning

confidence: 68%

The Saccharide Chain of Lupin Seed Conglutin γ is not Responsible for the Protection of the Native Protein from Degradation by Trypsin, but Facilitates the Refolding of the Acid‐Treated Protein to the Resistant Conformation

Duranti¹,

Gius²,

Sessa³

et al. 1995

European Journal of Biochemistry

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Native glycosylated and enzymically deglycosylated conglutin γ (a lupin seed oligomeric protein) both showed an unusual resistance to tryptic degradation. The result of this treatment was that a single 40–residue peptide was cleaved from the N‐terminus of conglutin γ light subunit. Acid treatment of the two protein forms led to their substantial unfolding, as indicated by CD spectra. After this treatment, both polypeptides were completely degraded by trypsin after a few minutes of incubation. Conversely, trypsin pulse experiments run under renaturing conditions demonstrated a different refolding behaviour of the two proteins: the glycosylated form became resistant to trypsin after a 7‐h renaturation, while the deglycosylated form required 42 h renaturation. These results were confirmed by CD spectra and reverse‐phase HPLC analyses of the glycosylated and deglycosylated conglutin γ forms. Therefore, it was concluded that the saccharide chain of conglutin γ increased the rate of formation of a trypsin‐resistant conformation upon refolding of the acid‐treated protein, without playing any direct role in the protection of the native protein from proteolysis.

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mentioning

confidence: 68%

The Saccharide Chain of Lupin Seed Conglutin γ is not Responsible for the Protection of the Native Protein from Degradation by Trypsin, but Facilitates the Refolding of the Acid‐Treated Protein to the Resistant Conformation

Duranti¹,

Gius²,

Sessa³

et al. 1995

European Journal of Biochemistry

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“…Moreover, a general protective role of XEGIP against biotic or abiotic stresses can be assumed, based on its wide expression in tomato vegetative tissues and high expression in cultured cells (Qin et al 2003). Leguminous seed proteins Bs7s and Cg have been considered as storage proteins, but more recent research indicates an additional physiological role as enhanced expression is observed in the response to heatshock (Duranti et al 1994;Kagawa and Hirano 1987) and both proteins have the capacity to bind specific proteins or peptides (Komatsu and Hirano 1991;Duranti et al 1995). Chromosomal location of TAXI-like genes PCR on nulli-tetrasomic lines located the identified TAXI-I sequence on wheat chromosome 3B of cv.…”

Section: Identification Of Taxi-like Genesmentioning

confidence: 99%

Molecular identification and chromosomal localization of genes encoding Triticum aestivum xylanase inhibitor I-like proteins in cereals

et al. 2004

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TAXI ( Triticum aestivum xylanase inhibitor) proteins are present in wheat flour and are known to inhibit glycosyl hydrolase family 11 endoxylanases, enzymes which are commonly applied in grain processing. Here, we describe the PCR-based molecular identification of genes encoding endoxylanase inhibitors HVXI and SCXI, the TAXI-like proteins from barley ( Hordeum vulgare) and rye ( Secale cereale) respectively. The HVXI coding sequence encodes a mature protein of 384 amino acids preceded by a 19 amino acid long signal sequence. SCXI-II/III has an open reading frame encoding a signal peptide of 21 amino acids and a mature protein of 375 amino acids. As for TAXI-I, no introns were detected in the untranslated regions and coding sequences identified. These newly identified sequences allowed us to perform a multiple sequence alignment with TAXI-I and similar proteins. Rice TAXI-type proteins clustered together with the cereal endoxylanase inhibitors. Dicotyledonous proteins with sequence similarity to TAXI-I, including the tomato xyloglucan-specific endoglucanase inhibiting protein, formed a different clade. The TAXI-type proteins may hence be part of a superfamily of proteins all involved in plant responses to biotic or abiotic stress and for which a function as glycosyl hydrolase inhibitors can be suggested. The chromosomal localization of the TAXI-I gene identified on wheat chromosome 3B, of the SCXI-II/III gene identified on rye chromosome 6R, and the presence of a cluster of TAXI-like genes on rice chromosome 1, allowed us to assign the location of TAXI-like genes to the wheat-rye translocation area 3BL/6RL characterized by RFLP markers XGlb33 and Xpsr454 and isozyme Est-5. In rice, RFLP marker C1310S corresponds to a TAXI-like protein encoding sequence.

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“…This study also reported that conglutin y could be immunoprecipitated from root extracts of germinating seedlings. These observations together led Duranti et al to conclude that conglutin y was a lectin (Duranti et al. 1995(Duranti et al.…”

Section: 35mentioning

confidence: 99%

“…The work in Italy and Australia continued between these groups dunng the 80's (Oram et at., 1981;Duranti et al, 198 U 984, 1988Duranti et al, 198 U 984, , 1990Restani et aI., 1981;Casero el al., 1983: Cerlctti el al., 1983: Lilley, 1986a, 1986b, 1986c: Lilley and Inglis, 1986; and has continued in Italy since that time (Duranti et al, 1991(Duranti et al, . 1992(Duranti et al, , 1994(Duranti et al, , 1995(Duranti et al, , 1996. A major interest in the biosynthesis and cDNNgene structure of the lupin proteins also emerged in Australia with reports by Gayler and others members of his group (Gayler etal., 1984(Gayler etal., ,1989(Gayler etal., ,1990Johnson eta!., 1985;Kolivas and Gayler, 1993;Ilgoutz and Gayler, 1995;Ilgoutz et al, 1997).…”

Section: Historical Perspectivementioning

confidence: 99%

“…This protein has been the focus of special attention, with the determination of the small subunit polypeptide amino acid sequence (Elleman, 1977) followed by a very thorough physicochemical study (Blagrove et al, 1980). These studies paved the way for specific studies of genetic effects (Oram et al, 1981), biosynthesis (Gayler et a!., 1984, Citharel and Delamarre, 1989: Deckert and Gwozdz, 1991, localization Gillespie, 1975: Gayler et al, 1989;Duranti et a!., 1991Duranti et a!., , 1994Duranti et a!., , 1996, possible lectin-like activity (Duranti et al, 1995(Duranti et al, , 1996 and behaviour on germination (Duranti et a!., 1984: Esnault et al, 1996. Conglutin y is one of only two lupin seed proteins to have been fully characterized at the precursor and cDNA levels (Kolivas and Gayler, 1993) and some understanding of gene transcription is emerging (Ilgoutz et a!., 1997).…”

Section: Conglutin Ymentioning

confidence: 99%

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Lupin Globulins

Lilley¹

1999

Seed Proteins

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Lectin-like activity of lupin seed conglutin γ, a glycoprotein previously referred to as a storage protein

Cited by 18 publications

References 19 publications

The Saccharide Chain of Lupin Seed Conglutin γ is not Responsible for the Protection of the Native Protein from Degradation by Trypsin, but Facilitates the Refolding of the Acid‐Treated Protein to the Resistant Conformation

The Saccharide Chain of Lupin Seed Conglutin γ is not Responsible for the Protection of the Native Protein from Degradation by Trypsin, but Facilitates the Refolding of the Acid‐Treated Protein to the Resistant Conformation

Molecular identification and chromosomal localization of genes encoding Triticum aestivum xylanase inhibitor I-like proteins in cereals

Lupin Globulins

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