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Cloning and characterisation of a novel P-glycoprotein homologue from barley

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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Cloning and characterisation of a novel P-glycoprotein homologue from barley. / Emyr Davies, T. G.; Theodoulou, Frederica L.; Hallahan, David L. et al.
In: Gene, Vol. 199, No. 1-2, 15.10.1997, p. 195-202.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Emyr Davies, TG, Theodoulou, FL, Hallahan, DL & Forde, BG 1997, 'Cloning and characterisation of a novel P-glycoprotein homologue from barley', Gene, vol. 199, no. 1-2, pp. 195-202. https://doi.org/10.1016/S0378-1119(97)00367-3

APA

Emyr Davies, T. G., Theodoulou, F. L., Hallahan, D. L., & Forde, B. G. (1997). Cloning and characterisation of a novel P-glycoprotein homologue from barley. Gene, 199(1-2), 195-202. https://doi.org/10.1016/S0378-1119(97)00367-3

Vancouver

Emyr Davies TG, Theodoulou FL, Hallahan DL, Forde BG. Cloning and characterisation of a novel P-glycoprotein homologue from barley. Gene. 1997 Oct 15;199(1-2):195-202. doi: 10.1016/S0378-1119(97)00367-3

Author

Emyr Davies, T. G. ; Theodoulou, Frederica L. ; Hallahan, David L. et al. / Cloning and characterisation of a novel P-glycoprotein homologue from barley. In: Gene. 1997 ; Vol. 199, No. 1-2. pp. 195-202.

Bibtex

@article{5295ceca44ea413e8fcd63cc8ca1f2cb,
title = "Cloning and characterisation of a novel P-glycoprotein homologue from barley",
abstract = "P-glycoproteins are members of a large superfamily of transport proteins (the 'traffic ATPases') that utilize ATP to translocate a wide range of substrates across biological membranes. Using a PCR-based approach, and degenerate oligonucleotides corresponding to conserved motifs, two 300-bp cDNA fragments (pBMDR1 and pBMDR2) with a significant sequence similarity to mammalian P-glycoproteins were amplified from barley (Hordeum vulgare) root poly A+ RNA and used as probes to screen a barley root cDNA library. A single full-length clone pHVMDR2 coding for a polypeptide of 1,232 residues (c. 134 kDa) was isolated. Comparison of this barley sequence with Arabidopsis ATPGP1 and human MDR1 and MDR3 P-glycoprotein sequences showed that the barley cDNA has 44%, 37% and 38% amino acid (aa) identity, respectively, with these sequences, and conserved structural features. RNase protection analysis showed that HVMDR2 mRNA is expressed at low levels in both barley roots and leaves. Southern blot analyses indicated that there is a small multigene family related to P-glycoproteins in barley. Possible functions for these barley P-glycoproteins are discussed.",
keywords = "ATP-binding cassette superfamily, Hordeum vulgare, Nucleotide sequence, PCR",
author = "{Emyr Davies}, {T. G.} and Theodoulou, {Frederica L.} and Hallahan, {David L.} and Forde, {Brian G.}",
year = "1997",
month = oct,
day = "15",
doi = "10.1016/S0378-1119(97)00367-3",
language = "English",
volume = "199",
pages = "195--202",
journal = "Gene",
issn = "0378-1119",
publisher = "Elsevier",
number = "1-2",

}

RIS

TY - JOUR

T1 - Cloning and characterisation of a novel P-glycoprotein homologue from barley

AU - Emyr Davies, T. G.

AU - Theodoulou, Frederica L.

AU - Hallahan, David L.

AU - Forde, Brian G.

PY - 1997/10/15

Y1 - 1997/10/15

N2 - P-glycoproteins are members of a large superfamily of transport proteins (the 'traffic ATPases') that utilize ATP to translocate a wide range of substrates across biological membranes. Using a PCR-based approach, and degenerate oligonucleotides corresponding to conserved motifs, two 300-bp cDNA fragments (pBMDR1 and pBMDR2) with a significant sequence similarity to mammalian P-glycoproteins were amplified from barley (Hordeum vulgare) root poly A+ RNA and used as probes to screen a barley root cDNA library. A single full-length clone pHVMDR2 coding for a polypeptide of 1,232 residues (c. 134 kDa) was isolated. Comparison of this barley sequence with Arabidopsis ATPGP1 and human MDR1 and MDR3 P-glycoprotein sequences showed that the barley cDNA has 44%, 37% and 38% amino acid (aa) identity, respectively, with these sequences, and conserved structural features. RNase protection analysis showed that HVMDR2 mRNA is expressed at low levels in both barley roots and leaves. Southern blot analyses indicated that there is a small multigene family related to P-glycoproteins in barley. Possible functions for these barley P-glycoproteins are discussed.

AB - P-glycoproteins are members of a large superfamily of transport proteins (the 'traffic ATPases') that utilize ATP to translocate a wide range of substrates across biological membranes. Using a PCR-based approach, and degenerate oligonucleotides corresponding to conserved motifs, two 300-bp cDNA fragments (pBMDR1 and pBMDR2) with a significant sequence similarity to mammalian P-glycoproteins were amplified from barley (Hordeum vulgare) root poly A+ RNA and used as probes to screen a barley root cDNA library. A single full-length clone pHVMDR2 coding for a polypeptide of 1,232 residues (c. 134 kDa) was isolated. Comparison of this barley sequence with Arabidopsis ATPGP1 and human MDR1 and MDR3 P-glycoprotein sequences showed that the barley cDNA has 44%, 37% and 38% amino acid (aa) identity, respectively, with these sequences, and conserved structural features. RNase protection analysis showed that HVMDR2 mRNA is expressed at low levels in both barley roots and leaves. Southern blot analyses indicated that there is a small multigene family related to P-glycoproteins in barley. Possible functions for these barley P-glycoproteins are discussed.

KW - ATP-binding cassette superfamily

KW - Hordeum vulgare

KW - Nucleotide sequence

KW - PCR

U2 - 10.1016/S0378-1119(97)00367-3

DO - 10.1016/S0378-1119(97)00367-3

M3 - Journal article

C2 - 9358056

AN - SCOPUS:0343742510

VL - 199

SP - 195

EP - 202

JO - Gene

JF - Gene

SN - 0378-1119

IS - 1-2

ER -