Complex formation regulates the glycosylation of the reversibly glycosylated polypeptide

Verónica De Pino, Mariela Borán, Lorena Norambuena, Mariela González, Francisca Reyes, Ariel Orellana, Silvia Moreno

Resultado de la investigación: Article

19 Citas (Scopus)

Resumen

Reversible glycosylated polypeptides (RGPs) are highly conserved plant-specific proteins, which can perform self-glycosylation. These proteins have been shown essential in plants yet its precise function remains unknown. In order to understand the function of this self-glycosylating polypeptide, it is important to establish what factors are involved in the regulation of the RGP activity. Here we show that incubation at high ionic strength produced a high self-glycosylation level and a high glycosylation reversibility of RGP from Solanum tuberosum L. In contrast, incubation at low ionic strength led to a low level of glycosylation and a low glycosylation reversibility of RGP. The incubation at low ionic strength favored the formation of high molecular weight RGP-containing forms, whereas incubation at high ionic strength produced active RGP with a molecular weight similar to the one expected for the monomer. Our data also showed that glycosylation of RGP, in its monomeric form, was highly reversible, whereas, a low reversibility of the protein glycosylation was observed when RGP was part of high molecular weight structures. In addition, glycosylation of RGP increased the occurrence of non-monomeric RGP-containing forms, suggesting that glycosylation may favor multimer formation. Finally, our results indicated that RGP from Arabidopsis thaliana and Pisum sativum are associated to golgi membranes, as part of protein complexes. A model for the regulation of the RGP activity and its binding to golgi membranes based on the glycosylation of the protein is proposed where the sugars linked to oligomeric form of RGP in the golgi may be transferred to acceptors involved in polysaccharide biosynthesis.

Idioma originalEnglish
Páginas (desde-hasta)335-345
Número de páginas11
PublicaciónPlanta
Volumen226
N.º2
DOI
EstadoPublished - 1 jul 2007

Huella dactilar

glycosylation
Glycosylation
polypeptides
Peptides
ionic strength
Osmolar Concentration
Molecular Weight
molecular weight
proteins
Plant Proteins
Membranes
Peas
Solanum tuberosum
Molecular Structure
Arabidopsis
Pisum sativum
Polysaccharides
Proteins
polysaccharides
Arabidopsis thaliana

ASJC Scopus subject areas

  • Genetics
  • Plant Science

Citar esto

De Pino, V., Borán, M., Norambuena, L., González, M., Reyes, F., Orellana, A., & Moreno, S. (2007). Complex formation regulates the glycosylation of the reversibly glycosylated polypeptide. Planta, 226(2), 335-345. https://doi.org/10.1007/s00425-007-0485-3
De Pino, Verónica ; Borán, Mariela ; Norambuena, Lorena ; González, Mariela ; Reyes, Francisca ; Orellana, Ariel ; Moreno, Silvia. / Complex formation regulates the glycosylation of the reversibly glycosylated polypeptide. En: Planta. 2007 ; Vol. 226, N.º 2. pp. 335-345.
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abstract = "Reversible glycosylated polypeptides (RGPs) are highly conserved plant-specific proteins, which can perform self-glycosylation. These proteins have been shown essential in plants yet its precise function remains unknown. In order to understand the function of this self-glycosylating polypeptide, it is important to establish what factors are involved in the regulation of the RGP activity. Here we show that incubation at high ionic strength produced a high self-glycosylation level and a high glycosylation reversibility of RGP from Solanum tuberosum L. In contrast, incubation at low ionic strength led to a low level of glycosylation and a low glycosylation reversibility of RGP. The incubation at low ionic strength favored the formation of high molecular weight RGP-containing forms, whereas incubation at high ionic strength produced active RGP with a molecular weight similar to the one expected for the monomer. Our data also showed that glycosylation of RGP, in its monomeric form, was highly reversible, whereas, a low reversibility of the protein glycosylation was observed when RGP was part of high molecular weight structures. In addition, glycosylation of RGP increased the occurrence of non-monomeric RGP-containing forms, suggesting that glycosylation may favor multimer formation. Finally, our results indicated that RGP from Arabidopsis thaliana and Pisum sativum are associated to golgi membranes, as part of protein complexes. A model for the regulation of the RGP activity and its binding to golgi membranes based on the glycosylation of the protein is proposed where the sugars linked to oligomeric form of RGP in the golgi may be transferred to acceptors involved in polysaccharide biosynthesis.",
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De Pino, V, Borán, M, Norambuena, L, González, M, Reyes, F, Orellana, A & Moreno, S 2007, 'Complex formation regulates the glycosylation of the reversibly glycosylated polypeptide', Planta, vol. 226, n.º 2, pp. 335-345. https://doi.org/10.1007/s00425-007-0485-3

Complex formation regulates the glycosylation of the reversibly glycosylated polypeptide. / De Pino, Verónica; Borán, Mariela; Norambuena, Lorena; González, Mariela; Reyes, Francisca; Orellana, Ariel; Moreno, Silvia.

En: Planta, Vol. 226, N.º 2, 01.07.2007, p. 335-345.

Resultado de la investigación: Article

TY - JOUR

T1 - Complex formation regulates the glycosylation of the reversibly glycosylated polypeptide

AU - De Pino, Verónica

AU - Borán, Mariela

AU - Norambuena, Lorena

AU - González, Mariela

AU - Reyes, Francisca

AU - Orellana, Ariel

AU - Moreno, Silvia

PY - 2007/7/1

Y1 - 2007/7/1

N2 - Reversible glycosylated polypeptides (RGPs) are highly conserved plant-specific proteins, which can perform self-glycosylation. These proteins have been shown essential in plants yet its precise function remains unknown. In order to understand the function of this self-glycosylating polypeptide, it is important to establish what factors are involved in the regulation of the RGP activity. Here we show that incubation at high ionic strength produced a high self-glycosylation level and a high glycosylation reversibility of RGP from Solanum tuberosum L. In contrast, incubation at low ionic strength led to a low level of glycosylation and a low glycosylation reversibility of RGP. The incubation at low ionic strength favored the formation of high molecular weight RGP-containing forms, whereas incubation at high ionic strength produced active RGP with a molecular weight similar to the one expected for the monomer. Our data also showed that glycosylation of RGP, in its monomeric form, was highly reversible, whereas, a low reversibility of the protein glycosylation was observed when RGP was part of high molecular weight structures. In addition, glycosylation of RGP increased the occurrence of non-monomeric RGP-containing forms, suggesting that glycosylation may favor multimer formation. Finally, our results indicated that RGP from Arabidopsis thaliana and Pisum sativum are associated to golgi membranes, as part of protein complexes. A model for the regulation of the RGP activity and its binding to golgi membranes based on the glycosylation of the protein is proposed where the sugars linked to oligomeric form of RGP in the golgi may be transferred to acceptors involved in polysaccharide biosynthesis.

AB - Reversible glycosylated polypeptides (RGPs) are highly conserved plant-specific proteins, which can perform self-glycosylation. These proteins have been shown essential in plants yet its precise function remains unknown. In order to understand the function of this self-glycosylating polypeptide, it is important to establish what factors are involved in the regulation of the RGP activity. Here we show that incubation at high ionic strength produced a high self-glycosylation level and a high glycosylation reversibility of RGP from Solanum tuberosum L. In contrast, incubation at low ionic strength led to a low level of glycosylation and a low glycosylation reversibility of RGP. The incubation at low ionic strength favored the formation of high molecular weight RGP-containing forms, whereas incubation at high ionic strength produced active RGP with a molecular weight similar to the one expected for the monomer. Our data also showed that glycosylation of RGP, in its monomeric form, was highly reversible, whereas, a low reversibility of the protein glycosylation was observed when RGP was part of high molecular weight structures. In addition, glycosylation of RGP increased the occurrence of non-monomeric RGP-containing forms, suggesting that glycosylation may favor multimer formation. Finally, our results indicated that RGP from Arabidopsis thaliana and Pisum sativum are associated to golgi membranes, as part of protein complexes. A model for the regulation of the RGP activity and its binding to golgi membranes based on the glycosylation of the protein is proposed where the sugars linked to oligomeric form of RGP in the golgi may be transferred to acceptors involved in polysaccharide biosynthesis.

KW - Golgi

KW - Plant polysaccharides

KW - Reversibly glycosylated polypeptide

KW - Self-glycosylation

KW - Xyloglucan

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U2 - 10.1007/s00425-007-0485-3

DO - 10.1007/s00425-007-0485-3

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JO - Planta

JF - Planta

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