The extensin signal peptide allows secretion of a heterologous protein from protoplasts

M De Loose; G Gheysen; C Tiré; J Gielen; R Villarroel; C Genetello; M Van Montagu; A Depicker; D Inzé

The extensin signal peptide allows secretion of a heterologous protein from protoplasts

M De Loose, G Gheysen, C Tiré, J Gielen, R Villarroel, C Genetello, M Van Montagu, A Depicker, D Inzé

Research output: Contribution to journal › A1: Web of Science-article › peer-review

Abstract

Extensins are hydroxyproline-rich glycoproteins which are amongst the most abundant proteins present in the cell wall of higher plants. Here, we describe the structural analysis of an extensin-encoding gene from Nicotiana plumbaginifolia. The encoded protein (46 kDa) has a highly repetitive structure and contains 37% proline, 18.1% tyrosine, 13.4% lysine, 8.1% serine and 7.1% histidine. The extensin-encoding sequence contains a typical signal peptide for translocation of the protein to the endoplasmic reticulum. By using chimeric genes consisting of different 5' parts of the extensin-encoding gene and the neomycin phosphotransferase II-encoding gene (nptII) as reporter gene, we show that the N-terminal part of extensin can mediate the secretion of NPTII from electroporated N. tabacum protoplasts.

Original language	English
Journal	Gene
Volume	99
Issue number	1
Pages (from-to)	95-100
Number of pages	6
ISSN	0378-1119
Publication status	Published - 1991

Keywords

Amino Acid Sequence
Base Sequence
Genes, Plant
Glycoproteins
Molecular Sequence Data
Plant Proteins
Plants, Toxic
Protein Conformation
Protein Sorting Signals
Protoplasts
Repetitive Sequences, Nucleic Acid
Restriction Mapping
Tobacco

Cite this

@article{4e1aa39076be45f4b42794cd9dcd73b1,

title = "The extensin signal peptide allows secretion of a heterologous protein from protoplasts",

abstract = "Extensins are hydroxyproline-rich glycoproteins which are amongst the most abundant proteins present in the cell wall of higher plants. Here, we describe the structural analysis of an extensin-encoding gene from Nicotiana plumbaginifolia. The encoded protein (46 kDa) has a highly repetitive structure and contains 37% proline, 18.1% tyrosine, 13.4% lysine, 8.1% serine and 7.1% histidine. The extensin-encoding sequence contains a typical signal peptide for translocation of the protein to the endoplasmic reticulum. By using chimeric genes consisting of different 5' parts of the extensin-encoding gene and the neomycin phosphotransferase II-encoding gene (nptII) as reporter gene, we show that the N-terminal part of extensin can mediate the secretion of NPTII from electroporated N. tabacum protoplasts.",

keywords = "Amino Acid Sequence, Base Sequence, Genes, Plant, Glycoproteins, Molecular Sequence Data, Plant Proteins, Plants, Toxic, Protein Conformation, Protein Sorting Signals, Protoplasts, Repetitive Sequences, Nucleic Acid, Restriction Mapping, Tobacco",

author = "{De Loose}, M and G Gheysen and C Tir{\'e} and J Gielen and R Villarroel and C Genetello and {Van Montagu}, M and A Depicker and D Inz{\'e}",

year = "1991",

language = "English",

volume = "99",

pages = "95--100",

journal = "Gene",

issn = "0378-1119",

publisher = "ELSEVIER SCIENCE BV",

number = "1",

}

TY - JOUR

T1 - The extensin signal peptide allows secretion of a heterologous protein from protoplasts

AU - De Loose, M

AU - Gheysen, G

AU - Tiré, C

AU - Gielen, J

AU - Villarroel, R

AU - Genetello, C

AU - Van Montagu, M

AU - Depicker, A

AU - Inzé, D

PY - 1991

Y1 - 1991

N2 - Extensins are hydroxyproline-rich glycoproteins which are amongst the most abundant proteins present in the cell wall of higher plants. Here, we describe the structural analysis of an extensin-encoding gene from Nicotiana plumbaginifolia. The encoded protein (46 kDa) has a highly repetitive structure and contains 37% proline, 18.1% tyrosine, 13.4% lysine, 8.1% serine and 7.1% histidine. The extensin-encoding sequence contains a typical signal peptide for translocation of the protein to the endoplasmic reticulum. By using chimeric genes consisting of different 5' parts of the extensin-encoding gene and the neomycin phosphotransferase II-encoding gene (nptII) as reporter gene, we show that the N-terminal part of extensin can mediate the secretion of NPTII from electroporated N. tabacum protoplasts.

AB - Extensins are hydroxyproline-rich glycoproteins which are amongst the most abundant proteins present in the cell wall of higher plants. Here, we describe the structural analysis of an extensin-encoding gene from Nicotiana plumbaginifolia. The encoded protein (46 kDa) has a highly repetitive structure and contains 37% proline, 18.1% tyrosine, 13.4% lysine, 8.1% serine and 7.1% histidine. The extensin-encoding sequence contains a typical signal peptide for translocation of the protein to the endoplasmic reticulum. By using chimeric genes consisting of different 5' parts of the extensin-encoding gene and the neomycin phosphotransferase II-encoding gene (nptII) as reporter gene, we show that the N-terminal part of extensin can mediate the secretion of NPTII from electroporated N. tabacum protoplasts.

KW - Amino Acid Sequence

KW - Base Sequence

KW - Genes, Plant

KW - Glycoproteins

KW - Molecular Sequence Data

KW - Plant Proteins

KW - Plants, Toxic

KW - Protein Conformation

KW - Protein Sorting Signals

KW - Protoplasts

KW - Repetitive Sequences, Nucleic Acid

KW - Restriction Mapping

KW - Tobacco

M3 - A1: Web of Science-article

C2 - 2022327

SN - 0378-1119

VL - 99

SP - 95

EP - 100

JO - Gene

JF - Gene

IS - 1

ER -

The extensin signal peptide allows secretion of a heterologous protein from protoplasts

Abstract

Keywords

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