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Un vínculo funcional entre la proteína similar a RuBisCO de Bacillus y el RuBisCO fotosintético
Hiroki Ashida1, Yohtaro Saito, Chojiro Kojima
1Graduate School of Biological Sciences, Nara Institute of Science and Technology (NAIST), 8916-5 Takayama, Ikoma, Nara 630-0101, Japan.
Science (New York, N.Y.)
|October 11, 2003
Resumen
Un bifosfato de ribulosa bacteriana carboxilasa / oxigenasa-como la proteína (RLP) de Bacillus subtilis facilita la vía de salvamento de la metionina. El RuBisCO fotosintético de Rhodospirillum rubrum puede reemplazar funcionalmente el B. subtilis RLP, destacando las capacidades enzimáticas conservadas.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Microbiología Microbiología.
- Enzimología Enzimología.
Sus antecedentes:
- Las bacterias no fotosintéticas y las arqueas poseen genes homólogos a la ribulosa bifosfato carboxilasa/oxigenasa (RuBisCO).
- Una proteína similar a RuBisCO (RLP) en Bacillus subtilis tiene una función no caracterizada.
Objetivo del estudio:
- Investigar la actividad enzimática de la proteína similar a RuBisCO (RLP) de B. subtilis.
- Para determinar si el RuBisCO fotosintético puede sustituir funcionalmente a la B. subtilis RLP en la vía de salvamento de la metionina.
Principales métodos:
- Se realizaron ensayos de actividad enzimática en el B. subtilis RLP.
- Se creó un mutante B. subtilis con un gen RLP interrumpido.
- El mutante fue complementado con el gen RuBisCO de Rhodospirillum rubrum.
Principales resultados:
- El B. subtilis RLP fue identificado como catalizador de la reacción de enolasa de 2,3-diketo-5-metiltiopentil-1-fosfato.
- La reacción ocurre dentro de la vía de salvamento de la metionina.
- El RuBisCO fotosintético de R. rubrum rescató el defecto de crecimiento del mutante B. subtilis RLP.
Conclusiones:
- El B. subtilis RLP juega un papel crucial en la vía de salvamento de la metionina.
- El RuBisCO fotosintético retiene la actividad funcional en la vía de salvamento de la metionina bacteriana, lo que demuestra una función enzimática conservada en diversos organismos.
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