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Epitope selection for multipeptide proteins: the case of RNA polymerase IV and V
ENRIQUE CASTAÑO DE LA SERNA
Acceso Abierto
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Large multipeptide protein complexes have provided a challenge for epitope selection, which is required for immunological protocols where native conformations are needed. Immunolocalization requires native conformation of the proteins, which is essential for further understanding of biological activity. RNA polymerase IV and V are multisubunit proteins that interact with other factors in the RNA-directed DNA methylation pathway for control of DNA silencing by small interfering RNA and DNA methylation. DNA silencing is an important process during cell differentiation, nuclear structure and viral control among others. RNA polymerase IV and V are yet to be studied in model monocot systems like Oryza sativa, which may provide further data to define if the genetic silencing mechanism has diverged over time as compared to dicots. Here we show anin silicoselection process of exposed sequences and their use for obtaining antibodies against native RNA polymerase IV and V inO. sativa.
29-07-2012
Artículo
BIOLOGÍA Y QUÍMICA
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