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Título: | Chemical synthesis of a fully active transcriptional repressor protein |
Autor: | Solar, Gloria del CSIC ORCID ; Albericio, Fernando CSIC ORCID; Eritja Casadellà, Ramón CSIC ORCID ; Espinosa, Manuel CSIC ORCID | Palabras clave: | Affinity purification Gel retardation assays In vitro transcription |
Fecha de publicación: | 24-may-1994 | Editor: | National Academy of Sciences (U.S.) | Citación: | Proceedings of the National Academy of Sciences of the USA 91(11): 5178-5182 (1994) | Resumen: | Plasmid pLS1-encoded 45-amino acid transcriptional repressor CopG (formerly RepA) has been chemically synthesized. A one-step purification of the synthetic protein has been developed, which yields high levels of pure protein with low or no contamination of truncated products. We have compared some properties of the chemical CopG protein with those of the biologically purified CopG. The two proteins were indistinguishable in (i) their ability to generate specific protein-DNA complexes, (ii) their capacity to protect a restriction site included within the CopG DNA target, and (iii) in their in vitro capacity to specifically repress synthesis of copG mRNA. | Descripción: | 5 pages, 5 figures.-- PMID: 8197204 [PubMed].-- PMCID: PMC43955. | Versión del editor: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC43955 | URI: | http://hdl.handle.net/10261/27458 | ISSN: | 0027-8424 | E-ISSN: | 1091-6490 |
Aparece en las colecciones: | (IQAC) Artículos |
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Solar_Gloria_et_al.pdf | 1,07 MB | Adobe PDF | Visualizar/Abrir |
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