Memórias do Instituto Oswaldo Cruz
Fundação Oswaldo Cruz, Fiocruz
Vol. 99, No. 7, 2004, pp. 733-737
Bioline Code: oc04148
Full paper language: English
Document type: Research Article
Document available free of charge
Memórias do Instituto Oswaldo Cruz, Vol. 99, No. 7, 2004, pp. 733-737
© Copyright 2004 - Instituto Oswaldo Cruz - Fiocruz.
Similarity between the Association Factor of Ribosomal Subunits and the Protein Stm1p from Saccharomyces cerevisiae|
Heriberto Correia; Rafael Medina; Alexandra Hernández; Ekaterina Bustamante; Kalpana Chakraburtty & Flor Herrera
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.
ribosomal association factor - Stm1p - G4 DNA - ribosomal function - G4p2 - triplex-DNA
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