Título:
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Biochemical organization of FtsZ in minimal membrane systems and cytomimetic crowded environments
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Autores:
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Sobrinos Sanguino, Marta
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Tipo de documento:
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texto impreso
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Editorial:
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Universidad Complutense de Madrid, 2018-06-19
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Dimensiones:
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application/pdf
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Nota general:
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info:eu-repo/semantics/openAccess
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Idiomas:
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Palabras clave:
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Estado = No publicado
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Materia = Ciencias: Química: Biología molecular
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Materia = Ciencias: Química: Bioquímica
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Tipo = Tesis
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Resumen:
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Bacterial division is an essential process highly regulated in time and space. In most bacteria, FtsZ is the major component of the divisome (molecular machinery effecting cytokinesis) which interacts with additional proteins that contribute to its function forming a dynamic ring at the midcell that is essential to constrict the membrane. FtsZ is a self-assembling GTPase, homolog of eukaryotic tubulin. The GTP-linked assembly and disassembly cycle of GTP is thought to be a key process in the formation of the division ring. The first molecular assembly of the divisome is the proto-ring, which in E. coli it is formed by FtsZ and the membrane tethering proteins ZipA, and FtsA. These proto-ring elements assemble at the cytoplasmic membrane forming a structure required for the incorporation of the remaining division proteins...
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En línea:
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https://eprints.ucm.es/id/eprint/51773/1/T40978.pdf
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