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Nueve modificaciones post-traduccionales durante la biosíntesis de la cinnamycin
Ayşe Ökesli1, Lisa E Cooper, Emily J Fogle
1Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, United States.
Journal of the American Chemical Society
|July 21, 2011
Resumen
Este estudio aclara la biosíntesis de la cinnamicina, un lantibiótico. Las enzimas clave CinX y CinM, junto con Cinorf7, son cruciales para formar sus puentes únicos de tioéter y lisinoalanina, esenciales para la actividad antimicrobiana.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología Molecular Biología Molecular
- Microbiología Microbiología.
Sus antecedentes:
- Los antibióticos son péptidos antimicrobianos con uniquísimos enlaces cruzados de tioéteres.
- La cinnamycin posee la lanthionine, la methyllanthionine, un puente de la lysinoalanine, y el ácido hidroxy-aspartic.
- Comprender la biosíntesis de la cinnamicina es clave para su función antimicrobiana.
Objetivo del estudio:
- Investigar el mecanismo biosintético de la cinnamicina.
- Caracterice los roles de CinX, CinM y Cinorf7 en las modificaciones post-traducionales.
- Determinar el orden y los requisitos de las actividades enzimáticas.
Principales métodos:
- Pruebas enzimáticas in vitro. ensayos enzimáticos en vitro. ensayos enzimáticos en vitro. ensayos enzimáticos en vitro. ensayos enzimáticos en vitro. ensayos enzimáticos en vitro. ensayos enzimáticos en vitro.
- Expresión heteróloga en Escherichia coli.
- Análisis de las modificaciones de los péptidos precursores.
Principales resultados:
- CinX hidroxilatos Asp15; CinM deshidrata Ser/Thr y cicliza los residuos de Cys para puentes (Me) Lan.
- El orden de actividad de CinX y CinM es intercambiable in vitro.
- Cinorf7 es esencial para la formación de puentes de lisinoalanina, que involucra a Lys19 y la deshidroalanina 6.
Conclusiones:
- El clúster de genes biosintéticos de la cinamicina codifica enzimas esenciales para sus modificaciones únicas.
- Se requieren enzimas específicas para la hidroxilación, la formación de puentes de tioéter y el enlace cruzado de lisinoalanina.
- La expresión heteróloga facilita el estudio de la biosíntesis lantibiótica.
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