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Variation in the ribosome interacting loop of the Sec61α from Giardia lamblia

The interaction between the ribosome and the endoplasmic reticulum-located Sec61 protein translocon is mediated through an arginine residue of Sec61α, which is conserved in all prokaryotic and eukaryotic orthologues characterized to date. Using in silico approaches we report that instead of arginine...

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Detalles Bibliográficos
Autores principales: Sinha, Abhishek, Ray, Atrayee, Ganguly, Sandipan, Ghosh Dastidar, Shubhra, Sarkar, Srimonti
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4588681/
https://www.ncbi.nlm.nih.gov/pubmed/26424409
http://dx.doi.org/10.1186/s13062-015-0087-0
Descripción
Sumario:The interaction between the ribosome and the endoplasmic reticulum-located Sec61 protein translocon is mediated through an arginine residue of Sec61α, which is conserved in all prokaryotic and eukaryotic orthologues characterized to date. Using in silico approaches we report that instead of arginine, this ribosome-interaction function is most likely discharged by a lysine residue in the protist Giardia lamblia. This functional substitution of the R with a K in GlSec61α may have taken place to accommodate a G-rich rRNA. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s13062-015-0087-0) contains supplementary material, which is available to authorized users.