On the interaction of ribosomal protein RPL22e with microtubules.
Cell Biol Int
; 43(7): 749-759, 2019 Jul.
Article
en En
| MEDLINE
| ID: mdl-30958636
Microtubule (MT) protein preparations often contain components of the translation machinery, including ribosome proteins. To understand the biological meaning of it we studied the interaction of ribosomal protein RPL22e with the MT. We found that bacteria expressed purified RPL22e-GFP-6His did co-sediment with brain tubulin MTs with 1.3 µM dissociation coefficient. Such a KD is comparable to some specific MT-associated proteins. Distinct in vitro interaction of RPL22e-GFP with MTs was also observed by TIRF microscopy. In real-time assay, RPL22e-GFP molecules stayed bound to MTs for several seconds, and 15% of them demonstrated random-walk along MTs with diffusion coefficient 0.03 µ2 /s. Deletion of basic areas of RPL22e did not have an impact on KD , and deletion of acidic tail slightly increased association with MTs. Interestingly, the deletion of acidic tail increased diffusion coefficient as well. The interaction of RPL22e with MTs is hardly noticeable in vivo in cultured cells, probably since a significant part of the protein is incorporated into the ribosomes. The mobility of ribosomal protein on the MTs probably prevents its interfering with MT-dependent transport and could ameliorate its transport to the nucleus.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas Ribosómicas
/
Tubulina (Proteína)
/
Proteínas de Unión al ARN
/
Microtúbulos
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Cell Biol Int
Año:
2019
Tipo del documento:
Article
País de afiliación:
Rusia
Pais de publicación:
Reino Unido