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Una nueva clase de inhibidores de la ARN polimerasa bacteriana afecta la adición de nucleótidos

Irina Artsimovitch¹, Clement Chu, A Simon Lynch

¹Department of Bacteriology, University of Wisconsin, Madison, WI 53706, USA.

Science (New York, N.Y.)

|October 25, 2003

Resumen

Nuevos inhibidores bacterianos de la ARN polimerasa (RNAP) revelan el mecanismo del ciclo de adición de nucleótidos de la enzima. Estos compuestos bloquean alostéricamente la catálisis al afectar los movimientos del sitio activo de la RNAP.

Área de la Ciencia:

Biología Molecular Biología Molecular
Enzimología Enzimología.
La bioquímica es la bioquímica.

Sus antecedentes:

La ARN polimerasa (RNAP) es crucial para la expresión génica.
El mecanismo preciso del ciclo de adición de nucleótidos de RNAP no se entiende completamente, a pesar de los datos estructurales existentes.

Objetivo del estudio:

Para dilucidar el mecanismo del ciclo de adición de nucleótidos de la ARN polimerasa bacteriana.
Caracterizar los nuevos inhibidores de la ARN polimerasa bacteriana (serie CBR703) y su modo de acción.

Principales métodos:

Caracterización de los inhibidores bacterianos de la RNAP (serie CBR703).
Pruebas que miden las actividades catalíticas de RNAP (adición de nucleótidos, pirofosforolisis, escisión de transcripción estimulada por Gre).
Análisis de las mutaciones de resistencia a CBR703 en RNAP.

Principales resultados:

Los compuestos CBR703 inhiben la adición de nucleótidos, la pirofosforolisis y la escisión de transcripción estimulada por Gre.
Estos inhibidores no afectan la translocación de ARN/ADN cuando están desacoplados de la catálisis.
Las mutaciones de resistencia se asignan a una superficie de RNAP opuesta al sitio activo, vinculada a través de una hélice puente.

Conclusiones:

Los inhibidores de CBR703 proporcionan información sobre el ciclo de adición de nucleótidos de RNAP.
Es probable que los compuestos actúen alostéricamente, impidiendo los movimientos del sitio activo esenciales para la catálisis.

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