Similarity between the association factor of ribosomal subunits and the protein Stm1p from Saccharomyces cerevisiae

Memórias do Instituto Oswaldo Cruz

Heriberto Correia²  Rafael Medina²  Alexandra Hernández²  Ekaterina Bustamante²  Kalpana Chakraburtty¹  Flor Herrera² 

[1] ,Universidad de Carabobo Facultad de Ciencias de la Salud Centro de Investigaciones BiomédicasMaracay Aragua ,Venezuela

关键词: ribosomal association factor;    Stm1p;    G4 DNA;    ribosomal function;    G4p2;    triplex-DNA;   

DOI  :  10.1590/S0074-02762004000700012

来源: SciELO

【 摘 要 】

A ribosome association factor (AF) was isolated from the yeast Sacchharomyces cerevisiae. Partial amino acid sequence of AF was determined from its fragment of 25 kDa isolated by treating AF with 2-(2-nitrophenylsulfenyl)-3-methyl-3'-Bromoindolenine (BNPS-skatole). This sequence has a 86% identity to the product of the single-copy S. cerevisiae STM1 gene that is apparently involved in several events like binding to quadruplex and triplex nucleic acids and participating in apoptosis, stability of telomere structures, cell cycle, and ribosomal function. Here we show that AF and Stm1p share some characteristics: both bind to quadruplex and Pu triplex DNA, associates ribosomal subunits, and are thermostable. These observations suggest that these polypeptides belong to a family of proteins that may have roles in the translation process.

【 授权许可】

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