Structural analysis of a plant sucrose carrier using monoclonal antibodies and bacteriophage lambda surface display.

Stolz J, Ludwig A, Stadler R, Biesgen C, Hagemann K, Sauer N (1999)


Publication Language: English

Publication Status: Published

Publication Type: Journal article, Original article

Publication year: 1999

Journal

Book Volume: 453

Pages Range: 375-379

Journal Issue: 3

DOI: 10.1016/S0014-5793(99)00756-5

Open Access Link: http://onlinelibrary.wiley.com/doi/10.1016/S0014-5793(99)00756-5/abstract

Abstract

Monoclonal antibodies were raised and selected against recombinant Plantago major PmSUC2 sucrose carrier protein. Epitopes of two monoclonal antibodies (PS2-1A2 and PS2-4D4) were mapped using N-terminally truncated PmSUC2 proteins and a lambda library displaying random PmSUC2 peptides. PS2-1A2 recognizes an octapeptide close to the N-terminus of PmSUC2, PS2-4D4 binds to a decapeptide at the very C-terminus. Analyses of antibody binding to yeast protoplasts with functionally active, tagged PmSUC2 protein revealed that both epitopes are located in cytoplasmic domains of PmSUC2. These results support a model for plant sucrose transporters containing 12 transmembrane helices with the N-terminus and the C-terminus on the cytoplasmic side of the plasma membrane.

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APA:

Stolz, J., Ludwig, A., Stadler, R., Biesgen, C., Hagemann, K., & Sauer, N. (1999). Structural analysis of a plant sucrose carrier using monoclonal antibodies and bacteriophage lambda surface display. Febs Letters, 453(3), 375-379. https://doi.org/10.1016/S0014-5793(99)00756-5

MLA:

Stolz, Jürgen, et al. "Structural analysis of a plant sucrose carrier using monoclonal antibodies and bacteriophage lambda surface display." Febs Letters 453.3 (1999): 375-379.

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